Microtubule - Knowledge (XXG)

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kinetochore, located in the center of each chromosome. Since each centrosome has a K fiber connecting to each pair of chromosomes, the chromosomes become tethered in the middle of the mitotic spindle by the K fibers. K fibers have a much longer half life than interpolar microtubules, at between 4 and 8 minutes. During the end of mitoses, the microtubules forming each K fiber begin to disassociate, thus shorting the K fibers. As the K fibers shorten the pair chromosomes are pulled apart right before cytokinesis. Previously, some researchers believed that K fibers form at their minus end originating from the centrosome just like other microtubules, however, new research has pointed to a different mechanism. In this new mechanism, the K fibers are initially stabilized at their plus end by the kinetochores and grow out from there. The minus end of these K fibers eventually connect to an existing Interpolar microtubule and are eventually connected to the centrosome in this way.

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and α-tubulin). So after the heterodimers are formed, they join together to form long chains that rise figuratively in one direction (e.g. upwards). These heterodimers, which are connected in a certain direction, form protofilaments. These long chains (protofilaments) now gradually accumulate next to each other so that a tube-like structure is formed, which has a lumen typical of a tube. Accordingly, mostly 13 protofilaments form the outer wall of the microtubules. The heterodimers consist of a positive and negative end, with alpha-tubulin forming the negative end and beta-tubulin the positive end. Due to the fact that the heterodimers are stacked on top of each other, there is always a negative and positive end. Microtubules grow by an addition of heterodimers at the plus end.

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there they interact with specific motor proteins which create force that pull the microtubules, and thus the entire centrosome towards the cell membrane. As stated above, this helps the centrosomes orient themselves away from each other in the cell. However these astral microtubules do not interact with the mitotic spindle itself. Experiments have shown that without these astral microtubules, the mitotic spindle can form, however its orientation in the cell is not always correct and thus mitosis does not occur as effectively. Another key function of the astral microtubules is to aid in cytokinesis. Astral microtubules interact with motor proteins at the cell membrane to pull the spindle and the entire cell apart once the chromosomes have been replicated.

306:. There are two distinct types of interactions that can occur between the subunits of lateral protofilaments within the microtubule called the A-type and B-type lattices. In the A-type lattice, the lateral associations of protofilaments occur between adjacent α and β-tubulin subunits (i.e. an α-tubulin subunit from one protofilament interacts with a β-tubulin subunit from an adjacent protofilament). In the B-type lattice, the α and β-tubulin subunits from one protofilament interact with the α and β-tubulin subunits from an adjacent protofilament, respectively. Experimental studies have shown that the B-type lattice is the primary arrangement within microtubules. However, in most microtubules there is a seam in which tubulin subunits interact α-β. 566:

on long-lived stable microtubules. Most of these modifications occur on the C-terminal region of alpha-tubulin. This region, which is rich in negatively charged glutamate, forms relatively unstructured tails that project out from the microtubule and form contacts with motors. Thus, it is believed that tubulin modifications regulate the interaction of motors with the microtubule. Since these stable modified microtubules are typically oriented towards the site of cell polarity in interphase cells, this subset of modified microtubules provide a specialized route that helps deliver vesicles to these polarized zones. These modifications include:

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retraction. When dynamics are suppressed, microtubules cannot remodel and, therefore, oppose the contractile forces. The morphology of cells with suppressed microtubule dynamics indicate that cells can extend the front edge (polarized in the direction of movement), but have difficulty retracting their trailing edge. On the other hand, high drug concentrations, or microtubule mutations that depolymerize the microtubules, can restore cell migration but there is a loss of directionality. It can be concluded that microtubules act both to restrain cell movement and to establish directionality.

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spontaneously pop out of the polymer. Since tubulin adds onto the end of the microtubule in the GTP-bound state, a cap of GTP-bound tubulin is proposed to exist at the tip of the microtubule, protecting it from disassembly. When hydrolysis catches up to the tip of the microtubule, it begins a rapid depolymerization and shrinkage. This switch from growth to shrinking is called a catastrophe. GTP-bound tubulin can begin adding to the tip of the microtubule again, providing a new cap and protecting the microtubule from shrinking. This is referred to as "rescue".

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are addition means of microtubule nucleation during mitosis. One of the most important of these additional means of microtubule nucleation is the RAN-GTP pathway. RAN-GTP associates with chromatin during mitosis to create a gradient that allows for local nucleation of microtubules near the chromosomes. Furthermore, a second pathway known as the augmin/HAUS complex (some organisms use the more studied augmin complex, while others such as humans use an analogous complex called HAUS) acts an additional means of microtubule nucleation in the mitotic spindle.

427:(MTOCs). Contained within the MTOC is another type of tubulin, γ-tubulin, which is distinct from the α- and β-subunits of the microtubules themselves. The γ-tubulin combines with several other associated proteins to form a lock washer-like structure known as the "γ-tubulin ring complex" (γ-TuRC). This complex acts as a template for α/β-tubulin dimers to begin polymerization; it acts as a cap of the (−) end while microtubule growth continues away from the MTOC in the (+) direction. 879: 664:. However, there are data to suggest that interference of microtubule dynamics is insufficient to block the cells undergoing mitosis. These studies have demonstrated that suppression of dynamics occurs at concentrations lower than those needed to block mitosis. Suppression of microtubule dynamics by tubulin mutations or by drug treatment have been shown to inhibit cell migration. Both microtubule stabilizers and destabilizers can suppress microtubule dynamics. 554: 31: 726:

microtubules increases the concentration of drug that is needed to suppress dynamics and inhibit cell migration. Thus, tumors that express β3-tubulin are not only resistant to the cytotoxic effects of microtubule targeted drugs, but also to their ability to suppress tumor metastasis. Moreover, expression of β3-tubulin also counteracts the ability of these drugs to inhibit angiogenesis which is normally another important facet of their action.

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microtubules, which have a half-life of 5–10 minutes, the captured microtubules can last for hours. This idea is commonly known as the "search and capture" model. Indeed, work since then has largely validated this idea. At the kinetochore, a variety of complexes have been shown to capture microtubule (+)-ends. Moreover, a (+)-end capping activity for interphase microtubules has also been described. This later activity is mediated by

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have the β-subunits exposed. These ends are designated the (−) and (+) ends, respectively. The protofilaments bundle parallel to one another with the same polarity, so, in a microtubule, there is one end, the (+) end, with only β-subunits exposed, while the other end, the (−) end, has only α-subunits exposed. While microtubule elongation can occur at both the (+) and (−) ends, it is significantly more rapid at the (+) end.

789:. MAP-2 proteins are located in the dendrites and in the body of neurons, where they bind with other cytoskeletal filaments. The MAP-4 proteins are found in the majority of cells and stabilize microtubules. In addition to MAPs that have a stabilizing effect on microtubule structure, other MAPs can have a destabilizing effect either by cleaving or by inducing depolymerization of microtubules. Three proteins called 769:, tau proteins have been shown to directly bind microtubules, promote nucleation and prevent disassembly, and to induce the formation of parallel arrays. Additionally, tau proteins have also been shown to stabilize microtubules in axons and have been implicated in Alzheimer's disease. The second class is composed of MAPs with a molecular weight of 200-1000 kDa, of which there are four known types: MAP-1, 1005: 253: 1204: 380: 887: 965: 348:, another component of the cytoskeleton. A microtubule is capable of growing and shrinking in order to generate force, and there are motor proteins that allow organelles and other cellular components to be carried along a microtubule. This combination of roles makes microtubules important for organizing and moving intracellular constituents. 613:: the addition of a glutamate polymer (typically 4-6 residues long) to the gamma-carboxyl group of any one of five glutamates found near the end of alpha-tubulin. Enzymes related to TTL add the initial branching glutamate (TTL4,5 and 7), while other enzymes that belong to the same family lengthen the polyglutamate chain (TTL6,11 and 13). 1024:

microtubules in the mitotic spindle can be characterized as interpolar. Furthermore, the half life of these microtubules is extremely short as it is less than one minute. Interpolar microtubules that do not attach to the kinetochores can aid in chromosome congregation through lateral interaction with the kinetochores.

1101:. Cilia and flagella always extend directly from a MTOC, in this case termed the basal body. The action of the dynein motor proteins on the various microtubule strands that run along a cilium or flagellum allows the organelle to bend and generate force for swimming, moving extracellular material, and other roles. 468:

which there is no longer any net assembly or disassembly at the end of the microtubule. If the dimer concentration is greater than the critical concentration, the microtubule will polymerize and grow. If the concentration is less than the critical concentration, the length of the microtubule will decrease.

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hydrolysis occurs in the globular head domains, which share similarities with the AAA+ (ATPase associated with various cellular activities) protein family. ATP hydrolysis in these domains is coupled to movement along the microtubule via the microtubule-binding domains. Dynein transports vesicles and

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Microtubules can act as substrates for motor proteins that are involved in important cellular functions such as vesicle trafficking and cell division. Unlike other microtubule-associated proteins, motor proteins utilize the energy from ATP hydrolysis to generate mechanical work that moves the protein

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on their tubulin subunits by the action of microtubule-bound enzymes. However, once the microtubule depolymerizes, most of these modifications are rapidly reversed by soluble enzymes. Since most modification reactions are slow while their reverse reactions are rapid, modified tubulin is only detected

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The sequence and exact composition of molecules during microtubule formation can thus be summarised as follows: A β-tubulin connects in the context of a non-existent covalent bond with an α-tubulin, which in connected form are a heterodimer, since they consist of two different polypeptides (β-tubulin

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Most of the microtubules that form the mitotic spindle originate from the centrosome. Originally it was thought that all of these microtubules originated from the centrosome via a method called search and capture, described in more detail in a section above, however new research has shown that there

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A final important note about the centrosomes and microtubules during mitosis is that while the centrosome is the MTOC for the microtubules necessary for mitosis, research has shown that once the microtubules themselves are formed and in the correct place the centrosomes themselves are not needed for

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group to lysine 40 of alpha-tubulin. This modification occurs on a lysine that is accessible only from the inside of the microtubule, and it remains unclear how enzymes access the lysine residue. The nature of the tubulin acetyltransferase remains controversial, but it has been found that in mammals

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Microtubules have a distinct polarity that is critical for their biological function. Tubulin polymerizes end to end, with the β-subunits of one tubulin dimer contacting the α-subunits of the next dimer. Therefore, in a protofilament, one end will have the α-subunits exposed while the other end will

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Expression of β3-tubulin has been reported to alter cellular responses to drug-induced suppression of microtubule dynamics. In general the dynamics are normally suppressed by low, subtoxic concentrations of microtubule drugs that also inhibit cell migration. However, incorporating β3-tubulin into

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shortly after assembly. The assembly properties of GDP-tubulin are different from those of GTP-tubulin, as GDP-tubulin is more prone to depolymerization. A GDP-bound tubulin subunit at the tip of a microtubule will tend to fall off, although a GDP-bound tubulin in the middle of a microtubule cannot

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can serve as an important platform for the nucleation of microtubules. Because nucleation from the centrosome is inherently symmetrical, Golgi-associated microtubule nucleation may allow the cell to establish asymmetry in the microtubule network. In recent studies, the Vale group at UCSF identified

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that associate laterally to form a single microtubule, which can then be extended by the addition of more α/β-tubulin dimers. Typically, microtubules are formed by the parallel association of thirteen protofilaments, although microtubules composed of fewer or more protofilaments have been observed

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are researched by fluorescently tagging a microtubule and fixing either the microtubule or motor proteins to a microscope slide, then visualizing the slide with video-enhanced microscopy to record the travel of the motor proteins. This allows the movement of the motor proteins along the microtubule

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disassembly, which is necessary for migration. It has been found that microtubules act as "struts" that counteract the contractile forces that are needed for trailing edge retraction during cell movement. When microtubules in the trailing edge of cell are dynamic, they are able to remodel to allow

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are a subclass of microtubules which only exist during and around mitosis. They originate from the centrosome, but do not interact with the chromosomes, kinetochores, or with the microtubules originating from the other centrosome. Instead their microtubules radiate towards the cell membrane. Once

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Most cells only have one centrosome for most of their cell cycle, however, right before mitosis, the centrosome duplicates, and the cell contains two centrosomes. Some of the microtubules that radiate from the centrosome grow directly away from the sister centrosome. These microtubules are called

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Plus end tracking proteins are MAP proteins which bind to the tips of growing microtubules and play an important role in regulating microtubule dynamics. For example, +TIPs have been observed to participate in the interactions of microtubules with chromosomes during mitosis. The first MAP to be

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Dynamic instability refers to the coexistence of assembly and disassembly at the ends of a microtubule. The microtubule can dynamically switch between growing and shrinking phases in this region. Tubulin dimers can bind two molecules of GTP, one of which can be hydrolyzed subsequent to assembly.

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also contain microtubules. The structure of these bacterial microtubules is similar to that of eukaryotic microtubules, consisting of a hollow tube of protofilaments assembled from heterodimers of bacterial tubulin A (BtubA) and bacterial tubulin B (BtubB). Both BtubA and BtubB share features of

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are the third important subclass of mitotic microtubules. These microtubules form direct connections with the kinetochores in the mitotic spindle. Each K fiber is composed of 20–40 parallel microtubules, forming a strong tube which is attached at one end to the centrosome and on the other to the

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proposed that microtubules use their dynamic properties of growth and shrinkage at their plus ends to probe the three dimensional space of the cell. Plus ends that encounter kinetochores or sites of polarity become captured and no longer display growth or shrinkage. In contrast to normal dynamic

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Following the initial nucleation event, tubulin monomers must be added to the growing polymer. The process of adding or removing monomers depends on the concentration of αβ-tubulin dimers in solution in relation to the critical concentration, which is the steady state concentration of dimers at

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and other mesenchymal cell-types, microtubules are anchored at the centrosome and radiate with their plus-ends outwards towards the cell periphery (as shown in the first figure). In these cells, the microtubules play important roles in cell migration. Moreover, the polarity of microtubules is

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are a class of microtubules which also radiate out from the centrosome during mitosis. These microtubules radiate towards the mitotic spindle, unlike astral microtubules. Interpolar microtubules are both the most abundant and dynamic subclass of microtubules during mitosis. Around 95 percent of

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The lateral association of the protofilaments generates a pseudo-helical structure, with one turn of the helix containing 13 tubulin dimers, each from a different protofilament. In the most common "13-3" architecture, the 13th tubulin dimer interacts with the next tubulin dimer with a vertical

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Microtubule polymers are extremely sensitive to various environmental effects. Very low levels of free calcium can destabilize microtubules and this prevented early researchers from studying the polymer in vitro. Cold temperatures also cause rapid depolymerization of microtubules. In contrast,

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The centrosome is critical to mitosis as most microtubules involved in the process originate from the centrosome. The minus ends of each microtubule begin at the centrosome, while the plus ends radiate out in all directions. Thus the centrosome is also important in maintaining the polarity of

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offset of 3 tubulin monomers due to the helicity of the turn. There are other alternative architectures, such as 11-3, 12-3, 14-3, 15-4, or 16-4, that have been detected at a much lower occurrence. Microtubules can also morph into other forms such as helical filaments, which are observed in

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astral microtubules. With the help of these astral microtubules the centrosomes move away from each other towards opposite sides of the cell. Once there, other types of microtubules necessary for mitosis, including interpolar microtubules and K-fibers can begin to form.

1143:) cause the reorganization of the microtubules so that their (-) ends are located in the lower part of the oocyte, polarizing the structure and leading to the appearance of an anterior-posterior axis. This involvement in the body's architecture is also seen in 1183:

has been described, which has provided information on the differential expression of the genes depending on the presence of these factors. This communication between the cytoskeleton and the regulation of the cellular response is also related to the action of

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are able to bind to tubulin and modify its assembly properties. These drugs can have an effect at intracellular concentrations much lower than that of tubulin. This interference with microtubule dynamics can have the effect of stopping a cell's

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is composed of two identical heavy chains, which make up two large globular head domains, and a variable number of intermediate and light chains. Dynein-mediated transport takes place from the (+) end towards the (-) end of the microtubule.

619:: the addition of a glycine polymer (2-10 residues long) to the gamma-carboxyl group of any one of five glutamates found near the end of beta-tubulin. TTL3 and 8 add the initial branching glycine, while TTL10 lengthens the polyglycine chain. 355:, the minus-ends of the microtubule polymer are anchored near the site of cell-cell contact and organized along the apical-basal axis. After nucleation, the minus-ends are released and then re-anchored in the periphery by factors such as 984:, oriented at right angles to each other. The centriole is formed from 9 main microtubules, each having two partial microtubules attached to it. Each centriole is approximately 400 nm long and around 200 nm in circumference. 451:

the protein complex augmin as a critical factor for centrosome-dependent, spindle-based microtubule generation. It that has been shown to interact with γ-TuRC and increase microtubule density around the mitotic spindle origin.

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Microtubules are one of the cytoskeletal filament systems in eukaryotic cells. The microtubule cytoskeleton is involved in the transport of material within cells, carried out by motor proteins that move on the surface of the

761:(MAPs) are present. The originally identified MAPs from brain tissue can be classified into two groups based on their molecular weight. This first class comprises MAPs with a molecular weight below 55-62 kDa, and are called 687:

Taxanes (alone or in combination with platinum derivatives (carboplatine) or gemcitabine) are used against breast and gynecological malignancies, squamous-cell carcinomas (head-and-neck cancers, some lung cancers), etc.

683:) block dynamic instability by stabilizing GDP-bound tubulin in the microtubule. Thus, even when hydrolysis of GTP reaches the tip of the microtubule, there is no depolymerization and the microtubule does not shrink back. 3554:

Bramblett GT, Goedert M, Jakes R, Merrick SE, Trojanowski JQ, Lee VM (June 1993). "Abnormal tau phosphorylation at Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding".

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parasites, have a MTOC but it is permanently found at the base of a flagellum. Here, nucleation of microtubules for structural roles and for generation of the mitotic spindle is not from a canonical centriole-like MTOC.

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Wen Y, Eng CH, Schmoranzer J, Cabrera-Poch N, Morris EJ, Chen M, Wallar BJ, Alberts AS, Gundersen GG (September 2004). "EB1 and APC bind to mDia to stabilize microtubules downstream of Rho and promote cell migration".

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The cellular cytoskeleton is a dynamic system that functions on many different levels: In addition to giving the cell a particular form and supporting the transport of vesicles and organelles, it can also influence

271:. The inner space of the hollow microtubule cylinders is referred to as the lumen. The α and β-tubulin subunits are ~50% identical at the amino acid level, and both have a molecular weight of approximately 50 kDa. 1008:

This diagram depicts the organization of a typical mitotic spindle found in animal cells. Shown here are the three main types of microtubules during mitosis and how they are oriented in the cell and the mitotic

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has a similar structure to dynein. Kinesin is involved in the transport of a variety of intracellular cargoes, including vesicles, organelles, protein complexes, and mRNAs toward the microtubule's (+)

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Paturle-Lafanechère L, Eddé B, Denoulet P, Van Dorsselaer A, Mazarguil H, Le Caer JP, Wehland J, Job D (October 1991). "Characterization of a major brain tubulin variant which cannot be tyrosinated".

324:. Unlike eukaryotic microtubules, bacterial microtubules do not require chaperones to fold. In contrast to the 13 protofilaments of eukaryotic microtubules, bacterial microtubules comprise only five. 340:. The roles of the microtubule cytoskeleton include mechanical support, organization of the cytoplasm, transport, motility and chromosome segregation. In developing neurons microtubules are known as 581:

at the new C-terminus. As a result, microtubules that accumulate this modification are often referred to as Glu-microtubules. Although the tubulin carboxypeptidase has yet to be identified, the

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Mikhailov A, Gundersen GG (1998). "Relationship between microtubule dynamics and lamellipodium formation revealed by direct imaging of microtubules in cells treated with nocodazole or taxol".

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Delta2: the removal of the last two residues from the C-terminus of alpha-tubulin. Unlike detyrosination, this reaction is thought to be irreversible and has only been documented in neurons.

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binds to the (+) growing end of the microtubules. Eribulin exerts its anticancer effects by triggering apoptosis of cancer cells following prolonged and irreversible mitotic blockade.

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mechanisms involved in this communication are little understood. However, the relationship between the drug-mediated depolymerization of microtubules, and the specific expression of

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Some cell types, such as plant cells, do not contain well defined MTOCs. In these cells, microtubules are nucleated from discrete sites in the cytoplasm. Other cell types, such as

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Animation of the microtubule dynamic instability. Tubulin dimers bound to GTP (red) bind to the growing end of a microtubule and subsequently hydrolyze GTP into GDP (blue).

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that can then associate laterally to form a hollow tube, the microtubule. The most common form of a microtubule consists of 13 protofilaments in the tubular arrangement.

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organelles throughout the cytoplasm. In order to do this, dynein molecules bind organelle membranes via a protein complex that contains a number of elements including

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Waterman-Storer CM, Worthylake RA, Liu BP, Burridge K, Salmon ED (May 1999). "Microtubule growth activates Rac1 to promote lamellipodial protrusion in fibroblasts".

4653: 1158:, where tubulin's dynamics and those of the associated proteins (such as the microtubule-associated proteins) are finely controlled during the development of the 3386:"Beta3-Tubulin Is Critical for Microtubule Dynamics, Cell Cycle Regulation, and Spontaneous Release of Microvesicles in Human Malignant Melanoma Cells (A375)" 1068:

Dynamic instability of microtubules is also required for the migration of most mammalian cells that crawl. Dynamic microtubules regulate the levels of key

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Weisenberg RC, Deery WJ, Dickinson PJ (September 1976). "Tubulin-nucleotide interactions during the polymerization and depolymerization of microtubules".

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70 (cytoplasmic linker protein), which has been shown to play a role in microtubule depolymerization rescue events. Additional examples of +TIPs include

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Although most microtubules have a half-life of 5–10 minutes, certain microtubules can remain stable for hours. These stabilized microtubules accumulate

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Ezratty EJ, Partridge MA, Gundersen GG (June 2005). "Microtubule-induced focal adhesion disassembly is mediated by dynamin and focal adhesion kinase".

502:-bound state. The GTP bound to α-tubulin is stable and it plays a structural function in this bound state. However, the GTP bound to β-tubulin may be 3122:

Hubbert C, Guardiola A, Shao R, Kawaguchi Y, Ito A, Nixon A, Yoshida M, Wang XF, Yao TP (May 2002). "HDAC6 is a microtubule-associated deacetylase".

485: 2942:"The chemical complexity of cellular microtubules: tubulin post-translational modification enzymes and their roles in tuning microtubule functions" 3629:

Molecular Neurobiology: Mechanisms Common to Brain, Skin and Immune System. Series: Progress in Clinical and Biological Research. Willey-Liss, Inc

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Burgess J, Northcote DH (September 1969). "Action of colchicine and heavy water on the polymerization of microtubules in wheat root meristem".

2046:"Maintenance of electrostatic stabilization in altered tubulin lateral contacts may facilitate formation of helical filaments in foraminifera" 1109:. However, prokaryotic flagella are entirely different in structure from eukaryotic flagella and do not contain microtubule-based structures. 2802:

Palazzo AF, Cook TA, Alberts AS, Gundersen GG (August 2001). "mDia mediates Rho-regulated formation and orientation of stable microtubules".

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van Eeden F, St Johnston D (August 1999). "The polarisation of the anterior-posterior and dorsal-ventral axes during Drosophila oogenesis".

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Jiang S, Narita A, Popp D, Ghoshdastider U, Lee LJ, Srinivasan R, Balasubramanian MK, Oda T, Koh F, Larsson M, Robinson RC (March 2016).

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Zhao B, Meka DP, Scharrenberg R, König T, Schwanke B, Kobler O, Windhorst S, Kreutz MR, Mikhaylova M, Calderon de Anda F (August 2017).

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Khodjakov, A., Cole, R. W., Oakley, B. R. and Rieder, C. L. (2000). "Centrosome-independent mitotic spindle formation in vertebrates".

363:. In this manner, they can facilitate the transport of proteins, vesicles and organelles along the apical-basal axis of the cell. In 968:

A 3D diagram of a centriole. Each circle represents one microtubule. In total there are 27 microtubules organized into 9 bundles of 3.

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cells, microtubules are disproportionately oriented from the MTOC toward the site of polarity, such as the leading edge of migrating

797:, and fidgetin have been observed to regulate the number and length of microtubules via their destabilizing activities. Furthermore, 1151: 600: 2459:"The augmin complex plays a critical role in spindle microtubule generation for mitotic progression and cytokinesis in human cells" 4188: 2254: 2892:

Janke C, Bulinski JC (November 2011). "Post-translational regulation of the microtubule cytoskeleton: mechanisms and functions".

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in order to establish the axis of the egg. Signals sent between the follicular cells and the oocyte (such as factors similar to

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Nucleation is the event that initiates the formation of microtubules from the tubulin dimer. Microtubules are typically

185:, and other proteins important for regulating microtubule dynamics. Recently an actin-like protein has been found in the 1251: 211:(1677). However, the fibrous nature of flagella and other structures were discovered two centuries later, with improved 3654:

Hirokawa N, Noda Y, Tanaka Y, Niwa S (October 2009). "Kinesin superfamily motor proteins and intracellular transport".

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is the primary MTOC of most cell types. However, microtubules can be nucleated from other sites as well. For example,

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Weisenberg RC (September 1972). "Microtubule formation in vitro in solutions containing low calcium concentrations".

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or the microtubule moving across the motor proteins. Consequently, some microtubule processes can be determined by

84: 3335:"Inhibition of cell migration and cell division correlates with distinct effects of microtubule inhibiting drugs" 3384:

Altonsy, Mohammed; Ganguly, Anutosh; Amrein, Matthias; Surmanowicz, Philip; Li, Shu; Lauzon, Gilles (Mar 2020).

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are in blue. The cytoskeleton provides the cell with an inner framework and enables it to move and change shape.

6913: 1683: 1136: 2197:"Microtubules in bacteria: Ancient tubulins build a five-protofilament homolog of the eukaryotic cytoskeleton" 1140: 1131: 114: 3791:""It takes two to tango": understanding how centrosome duplication is regulated throughout the cell cycle" 3627:

Hirokawa, N (1994). "The neuronal cytoskeleton: roles in neuronal morphogenesis and organelle transport".

3606: 1949: 1080:, which regulate cell contractility and cell spreading. Dynamic microtubules are also required to trigger 912: 785:

and C. The C protein plays an important role in the retrograde transport of vesicles and is also known as

499: 414: 191: 186: 148: 3234:"Reversible polyglutamylation of alpha- and beta-tubulin and microtubule dynamics in mouse brain neurons" 2706:

Cheeseman IM, Desai A (January 2008). "Molecular architecture of the kinetochore-microtubule interface".

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Tubulin and microtubule-mediated processes, like cell locomotion, were seen by early microscopists, like

6973: 6968: 5332: 4686: 1379: 1180: 1122: 657: 507: 369: 102: 2753: 5601: 3710: 3131: 3086: 2621: 2470: 2288: 2149: 2057: 1718: 1608: 1497: 757:. The rates of microtubule polymerization, depolymerization, and catastrophe vary depending on which 4574:"Modulation of the expression of connective tissue growth factor by alterations of the cytoskeleton" 6908: 5541: 4480:

Tucker RP (1990). "The roles of microtubule-associated proteins in brain morphogenesis: a review".

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Carmona, Bruno; Marinho, H. Susana; Matos, Catarina Lopes; Nolasco, Sofia; Soares, Helena (2023).

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Kirschner M, Mitchison T (May 1986). "Beyond self-assembly: from microtubules to morphogenesis".

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Image of a fibroblast cell containing fluorescently labeled actin (red) and microtubules (green).

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and have an inner diameter between 11 and 15 nm. They are formed by the polymerization of a

4525:"Cytoskeletal control of gene expression: depolymerization of microtubules activates NF-kappa B" 3232:

Audebert S, Desbruyères E, Gruszczynski C, Koulakoff A, Gros F, Denoulet P, Eddé B (June 1993).

2553: 2547: 1486:"Novel actin filaments from Bacillus thuringiensis form nanotubules for plasmid DNA segregation" 446:. In addition, work from the Kaverina group at Vanderbilt, as well as others, suggests that the 3519:

Mandelkow E, Mandelkow EM (February 1995). "Microtubules and microtubule-associated proteins".

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Walker RA, O'Brien ET, Pryer NK, Soboeiro MF, Voter WA, Erickson HP, Salmon ED (October 1988).

607:. The real impact of acetylation in the structure and function of microtubules remains elusive. 553: 6759: 6462: 5123: 4595: 4554: 4497: 4454: 4413: 4378: 4319: 4276: 4241: 4192: 4157: 4113: 4064: 4015: 3966: 3909: 3861: 3812: 3771: 3728: 3671: 3636: 3572: 3536: 3501: 3466: 3417: 3366: 3312: 3263: 3214: 3196: 3147: 3104: 3055: 3020: 2971: 2909: 2863: 2819: 2773: 2723: 2680: 2637: 2594: 2557: 2498: 2439: 2390: 2355: 2314: 2228: 2177: 2118: 2083: 2026: 1977: 1918: 1869: 1820: 1812: 1777: 1734: 1675: 1636: 1525: 1466: 1423: 1352: 1303: 610: 164: 6482: 256:

Cartoon representation of the structure of α(yellow)/β(red)-tubulin heterodimer, GTP and GDP.

6707: 6414: 6399: 6394: 6389: 6384: 6374: 6295: 6004: 5984: 5954: 5949: 5831: 5186: 5181: 4585: 4544: 4536: 4489: 4444: 4405: 4368: 4358: 4311: 4268: 4231: 4223: 4184: 4147: 4103: 4095: 4054: 4046: 4005: 3997: 3956: 3948: 3901: 3851: 3843: 3802: 3763: 3718: 3663: 3564: 3528: 3493: 3456: 3448: 3407: 3397: 3356: 3346: 3302: 3294: 3253: 3245: 3204: 3186: 3139: 3094: 3047: 3010: 3002: 2961: 2953: 2901: 2855: 2811: 2765: 2715: 2672: 2629: 2586: 2488: 2478: 2429: 2421: 2382: 2345: 2304: 2296: 2218: 2208: 2167: 2157: 2110: 2073: 2065: 2016: 2008: 1997:"Structural basis of interprotofilament interaction and lateral deformation of microtubules" 1967: 1959: 1908: 1900: 1889:"Lattice defects in microtubules: protofilament numbers vary within individual microtubules" 1859: 1851: 1804: 1769: 1726: 1667: 1626: 1616: 1515: 1505: 1458: 1413: 1342: 1334: 1293: 1285: 212: 137: 70: 6624: 6619: 6614: 6609: 6364: 6354: 6344: 6339: 6310: 6014: 6009: 5056: 4944: 4934: 4909: 4889: 4793: 4773: 128:, and intracellular macromolecular assemblies. They are also involved in cell division (by 6849: 5463: 5313: 5196: 5016: 1551: 1172: 1062: 616: 447: 388: 373: 315: 3937:"Asymmetric cell division: recent developments and their implications for tumour biology" 3714: 3209: 3174: 3135: 3090: 2625: 2474: 2292: 2153: 2061: 1722: 1612: 1501: 368:

acted upon by motor proteins, which organize many components of the cell, including the

6812: 6675: 5372: 5203: 4712: 4549: 4524: 4373: 4346: 4236: 4212:"Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton" 4211: 4108: 4083: 4059: 4034: 4010: 3985: 3961: 3936: 3856: 3831: 3461: 3436: 3412: 3385: 3361: 3334: 3307: 3282: 3073:

Kalebic N, Sorrentino S, Perlas E, Bolasco G, Martinez C, Heppenstall PA (2013-06-10).

3015: 2990: 2966: 2941: 2493: 2458: 2434: 2409: 2309: 2276: 2246: 2223: 2196: 2172: 2137: 2078: 2045: 2021: 1996: 1972: 1937: 1913: 1888: 1864: 1839: 1631: 1596: 1520: 1485: 1347: 1322: 1298: 1273: 1209: 1159: 1081: 624: 570: 520: 455: 4449: 4432: 4409: 3723: 3698: 3258: 3233: 1418: 1401: 753:

MAPs have been shown to play a crucial role in the regulation of microtubule dynamics

6962: 6876: 6871: 5836: 5706: 5655: 5605: 5545: 5467: 5435: 5376: 5162: 4681: 4493: 4084:"Genome stability is ensured by temporal control of kinetochore-microtubule dynamics" 3568: 3532: 3437:"Class III β-Tubulin Counteracts the Ability of Paclitaxel to Inhibit Cell Migration" 2676: 2114: 1217: 1185: 1118: 936: 636: 628: 524: 275: 268: 228: 171: 98: 66: 4509: 4466: 4331: 4288: 4136:"Microtubule assembly during mitosis - from distinct origins to distinct functions?" 3740: 3683: 3584: 2875: 2735: 2692: 2649: 2386: 1808: 1773: 1746: 1435: 1061:. This configuration is thought to help deliver microtubule-bound vesicles from the 6720: 5775: 5530: 5074: 4666: 3921: 3159: 2921: 2831: 2457:

Uehara R, Nozawa RS, Tomioka A, Petry S, Vale RD, Obuse C, Goshima G (April 2009).

944: 940: 932: 762: 715:

have the opposite effect, blocking the polymerization of tubulin into microtubules.

443: 396: 392: 333: 303: 160: 50: 30: 6692: 6670: 3298: 2754:"Detyrosinated (Glu) microtubules are stabilized by an ATP-sensitive plus-end cap" 1730: 895:

along the substrate. The major motor proteins that interact with microtubules are

252: 2989:

Ersfeld K, Wehland J, Plessmann U, Dodemont H, Gerke V, Weber K (February 1993).

2213: 1544: 1449:

Howard J, Hyman AA (February 2007). "Microtubule polymerases and depolymerases".

1053:

Microtubule plus ends are often localized to particular structures. In polarized

980:) of the cell during mitosis. Each centrosome is made up of two cylinders called 6866: 6817: 6687: 6577: 5351: 5306: 5225: 5147: 4695: 3892:

Rosenblatt J (March 2005). "Spindle assembly: asters part their separate ways".

1004: 731: 708: 697: 632: 591: 341: 208: 97:. They are involved in maintaining the structure of the cell and, together with 4631: 2517: 2463:

Proceedings of the National Academy of Sciences of the United States of America

2300: 2142:

Proceedings of the National Academy of Sciences of the United States of America

2138:"Structure of bacterial tubulin BtubA/B: evidence for horizontal gene transfer" 1621: 1490:

Proceedings of the National Academy of Sciences of the United States of America

1203: 379: 117:

and are involved in a variety of cellular processes, including the movement of

6918: 6837: 6827: 6715: 5826: 5805: 5571: 5508: 5503: 5498: 5478: 5453: 5441: 5427: 5422: 5417: 5412: 5407: 5402: 5397: 5392: 5387: 5249: 5131: 5120: 5106: 4722: 2612:

Mitchison T, Kirschner M (1984). "Dynamic instability of microtubule growth".

2012: 1566: 1462: 1323:"Organization of neuronal microtubules in the nematode Caenorhabditis elegans" 1199: 1155: 1102: 1069: 1058: 1054: 973: 886: 712: 704: 693: 676: 653: 503: 431: 384: 364: 278: 199:

segregation. Other bacterial microtubules have a ring of five protofilaments.

156: 141: 58: 54: 4227: 3200: 1816: 1597:"MTrack: Automated Detection, Tracking, and Analysis of Dynamic Microtubules" 1243: 6747: 6742: 6737: 6697: 6535: 6530: 6525: 5883: 5863: 5518: 5513: 5493: 5488: 5483: 5473: 5382: 5286: 5220: 4621: 4363: 3754:

Pereira G, Schiebel E (February 1997). "Centrosome-microtubule nucleation".

3452: 3351: 3191: 3175:"Tubulin Post-Translational Modifications: The Elusive Roles of Acetylation" 2769: 2483: 2410:"Microtubule network asymmetry in motile cells: role of Golgi-derived array" 2195:

Pilhofer M, Ladinsky MS, McDowall AW, Petroni G, Jensen GJ (December 2011).

2162: 1855: 1510: 1098: 981: 680: 661: 578: 352: 337: 261: 241: 195:, which forms a microtubule-like structure called a nanotubule, involved in 125: 118: 62: 17: 4599: 4590: 4573: 4540: 4417: 4382: 4323: 4280: 4161: 4117: 4068: 3970: 3913: 3865: 3816: 3732: 3675: 3470: 3421: 3370: 3316: 3218: 3151: 3108: 2975: 2913: 2867: 2823: 2777: 2727: 2502: 2443: 2359: 2318: 2232: 2181: 2122: 2087: 2030: 1963: 1904: 1873: 1795:

Desai, A.; Mitchison, T. J. (1997). "Microtubule polymerization dynamics".

1679: 1671: 1640: 1529: 1470: 1427: 1307: 4558: 4501: 4458: 4245: 4196: 4019: 4001: 3847: 3775: 3767: 3640: 3576: 3540: 3505: 3267: 3059: 3024: 3006: 2684: 2641: 2394: 1981: 1922: 1824: 1781: 1738: 1125:. For example, a network of polarized microtubules is required within the 947:) that require access to the nucleus to replicate their genomes attach to 105:, they form the cytoskeleton. They also make up the internal structure of 6861: 6822: 6754: 6727: 6594: 6582: 6457: 6452: 5893: 5888: 5810: 5244: 5239: 5101: 4572:

Ott C, Iwanciw D, Graness A, Giehl K, Goppelt-Struebe M (November 2003).

3402: 2598: 2425: 1356: 1338: 1289: 917: 813: 809: 718: 574: 439: 420: 223: 110: 3986:"Kinetochore microtubule dynamics and the metaphase-anaphase transition" 3905: 3497: 3249: 3051: 2590: 964: 351:

The organization of microtubules in the cell is cell-type specific. In

6888: 6842: 6732: 6662: 6631: 6561: 6556: 6520: 6515: 6510: 6477: 6447: 6442: 6437: 6432: 6117: 6049: 6044: 6039: 6034: 6029: 5921: 5858: 5346: 5291: 5232: 5215: 5176: 4662: 4152: 4135: 3807: 3790: 3099: 3074: 2752:

Infante AS, Stein MS, Zhai Y, Borisy GG, Gundersen GG (November 2000).

923: 896: 794: 790: 529: 360: 321: 299: 265: 236: 196: 182: 178: 133: 129: 74: 46: 42: 2350: 2333: 2069: 6807: 6789: 6784: 6779: 6774: 6764: 6599: 6492: 6487: 6472: 6467: 6379: 6325: 6290: 6265: 6260: 6255: 6250: 6240: 6235: 6225: 6210: 6205: 6087: 6082: 6077: 5989: 5979: 5959: 5944: 5939: 5934: 5929: 5795: 5566: 5561: 5318: 4984: 4979: 4969: 4747: 4626: 4189:

10.1002/(SICI)1097-0169(1998)41:4<325::AID-CM5>3.0.CO;2-D

2957: 2815: 2633: 2373:

Desai A, Mitchison TJ (1997). "Microtubule polymerization dynamics".

2277:"Microtubules Modulate F-actin Dynamics during Neuronal Polarization" 1760:

Desai A, Mitchison TJ (1997). "Microtubule polymerization dynamics".

1144: 1126: 1094: 907: 900: 867: 863: 843: 839: 835: 786: 672: 595: 540:, a protein that tracks along the growing plus ends of microtubules. 537: 356: 232: 174: 4315: 4099: 4050: 3952: 3667: 3143: 2905: 2859: 2719: 1655: 1595:

Kapoor V, Hirst WG, Hentschel C, Preibisch S, Reber S (March 2019).

2518:"The Self-Assembly and Dynamic Structure of Cytoskeletal Filaments" 2516:

Alberts B, Johnson A, Lewis J, Raff M, Roberts K, Walter P (2002).

2101:

Nogales E (2000). "Structural insights into microtubule function".

6832: 6604: 6587: 6424: 6419: 6409: 6404: 6369: 6359: 6349: 6334: 6315: 6305: 6300: 6285: 6280: 6275: 6270: 6245: 6230: 6220: 6215: 6200: 6195: 6175: 6170: 6165: 6160: 6155: 6150: 6145: 6140: 6135: 6130: 6125: 6097: 6092: 6059: 6054: 6024: 6019: 5999: 5994: 5974: 5964: 5879: 5757: 5752: 5747: 5742: 5737: 5732: 5727: 5722: 5717: 5712: 5696: 5691: 5686: 5681: 5676: 5671: 5666: 5661: 5636: 5631: 5626: 5621: 5616: 5611: 5591: 5586: 5581: 5576: 5556: 5551: 5261: 5191: 5140: 5137: 5134: 5126: 5115: 5112: 5109: 5094: 5089: 5084: 5079: 5051: 5041: 5026: 4959: 4949: 4929: 4904: 4899: 4884: 4874: 4869: 4864: 4859: 4854: 4849: 4834: 4788: 4783: 4778: 4768: 4763: 4758: 4737: 4732: 4727: 4717: 4704: 1840:"A microtubule bestiary: structural diversity in tubulin polymers" 885: 877: 859: 851: 847: 831: 782: 778: 604: 552: 480: 435: 378: 345: 251: 106: 83: 4345:

Ganguly A, Yang H, Sharma R, Patel KD, Cabral F (December 2012).

4272: 899:, which usually moves toward the (+) end of the microtubule, and 264:, microtubules are long, hollow cylinders made up of polymerized 170:

There are many proteins that bind to microtubules, including the

6933: 6928: 6923: 6883: 6854: 6769: 6646: 6641: 6636: 6540: 6190: 6185: 6180: 6107: 6102: 5969: 5851: 5846: 5841: 5301: 5296: 5254: 5167: 5157: 5152: 5046: 5036: 5031: 5021: 5011: 5006: 5001: 4996: 4919: 4844: 4839: 4829: 4824: 4819: 4814: 4809: 4804: 4082:

Bakhoum SF, Thompson SL, Manning AL, Compton DA (January 2009).

1189: 1106: 1077: 1073: 855: 805: 777:. MAP-1 proteins consists of a set of three different proteins: 774: 770: 648: 4635: 4347:"The role of microtubules and their dynamics in cell migration" 1887:

Chrétien D, Metoz F, Verde F, Karsenti E, Wade RH (June 1992).

3598: 3435:

Ganguly, Anutosh; Yang, Hailing; Fernando, Gabral (May 2011).

3283:"Paclitaxel-dependent cell lines reveal a novel drug activity" 4035:"Chromosome congression in the absence of kinetochore fibres" 1656:"Refined structure of alpha beta-tubulin at 3.5 A resolution" 1117:

The cytoskeleton formed by microtubules is essential to the

603:. however, the reverse reaction is known to be catalyzed by 4033:

Cai S, O'Connell CB, Khodjakov A, Walczak CE (July 2009).

1402:"The molecular motor toolbox for intracellular transport" 804:

MAPs are determinants of different cytoskeletal forms of

3832:"The mechanics of microtubule networks in cell division" 3075:"αTAT1 is the major α-tubulin acetyltransferase in mice" 2044:

Bassen DM, Hou Y, Bowser SS, Banavali NK (August 2016).

1093:

Microtubules have a major structural role in eukaryotic

667:

The drugs that can alter microtubule dynamics include:

2136:

Schlieper D, Oliva MA, Andreu JM, Löwe J (June 2005).

27:

Polymer of tubulin that forms part of the cytoskeleton

1654:

Löwe J, Li H, Downing KH, Nogales E (November 2001).

1150:

Another area where microtubules are essential is the

498:

During polymerization, the tubulin dimers are in the

2549:

Cell and Molecular Biology: Concepts and Experiments

6901: 6800: 6706: 6661: 6570: 6549: 6501: 6324: 6116: 6068: 5920: 5906: 5872: 5819: 5788: 5768: 5647: 5529: 5360: 5342: 5331: 5274: 5067: 4746: 4703: 4694: 4680: 4673: 4622:

3D microtubule structures in the EM Data Bank(EMDB)

93:Microtubules play an important role in a number of 3984:Zhai Y, Kronebusch PJ, Borisy GG (November 1995). 2408:Vinogradova T, Miller PM, Kaverina I (July 2009). 882:A cytoplasmic dynein motor bound to a microtubule. 801:is predicted to be localized to the microtubules. 4433:"Axis development and early asymmetry in mammals" 4210:Ren XD, Kiosses WB, Schwartz MA (February 1999). 3699:"Cell division: The renaissance of the centriole" 2991:"Characterization of the tubulin-tyrosine ligase" 2334:"Generation of noncentrosomal microtubule arrays" 159:found in the center of many animal cells or the 4129: 4127: 3328: 3326: 2935: 2933: 2931: 2887: 2885: 2747: 2745: 2375:Annual Review of Cell and Developmental Biology 1797:Annual Review of Cell and Developmental Biology 1762:Annual Review of Cell and Developmental Biology 812:, with microtubules being farther apart in the 1274:"A "microtubule" in plant cell fine structure" 57:cells. 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Brain Research Reviews 3941:Nature Reviews. Molecular Cell Biology 3656:Nature Reviews. Molecular Cell Biology 2940:Garnham CP, Roll-Mecak A (July 2012). 2894:Nature Reviews. Molecular Cell Biology 2708:Nature Reviews. Molecular Cell Biology 2552:. USA: John Wiley & Sons. p. 743:Microtubule-associated proteins (MAPs) 4627:Protocols for generating microtubules 3789:Hinchcliffe EH, Sluder G (May 2001). 825:Microtubule plus-end tracking protein 181:, microtubule-severing proteins like 7: 2247:"Medical Definition of Neurotubules" 286:in various species as well as 140:, which are used to pull eukaryotic 4578:The Journal of Biological Chemistry 4351:The Journal of Biological Chemistry 3339:The Journal of Biological Chemistry 948: 423:and organized by organelles called 136:) and are the main constituents of 53:and provide structure and shape to 4177:Cell Motility and the Cytoskeleton 1567:"Microtubule Motors and Movements" 903:, which moves toward the (−) end. 819:Plus-end tracking proteins (+TIPs) 544:Regulation of microtubule dynamics 25: 4523:Rosette C, Karin M (March 1995). 4134:Meunier S, Vernos I (June 2012). 1995:Sui H, Downing KH (August 2010). 1152:development of the nervous system 1028:K fibers/Kinetochore microtubules 5282:Wiskott–Aldrich syndrome protein 3830:Forth S, Kapoor TM (June 2017). 2115:10.1146/annurev.biochem.69.1.277 1376:Rensselaer Polytechnic Institute 1272:Ledbetter MC, Porter KR (1963). 1223:Orchestrated objective reduction 1202: 573:: the removal of the C-terminal 563:post-translational modifications 549:Post-translational modifications 442:have MTOCs at their base termed 6503:Microtubule organising proteins 3609:from the original on 2017-05-01 3521:Current Opinion in Cell Biology 2784:from the original on 2024-02-21 2528:from the original on 2018-06-05 2387:10.1146/annurev.cellbio.13.1.83 2257:from the original on 2018-09-27 1838:Chaaban S, Brouhard GJ (2017). 1809:10.1146/annurev.cellbio.13.1.83 1774:10.1146/annurev.cellbio.13.1.83 1686:from the original on 2021-01-22 1577:from the original on 2021-12-03 1451:Current Opinion in Cell Biology 1254:from the original on 2022-09-29 1190:connective tissue growth factor 759:microtubule-associated proteins 599:the major acetyltransferase is 34:Microtubule and tubulin metrics 1321:Chalfie M, Thomson JN (1979). 749:Microtubule-associated protein 425:microtubule-organizing centers 163:of cilia and flagella, or the 153:microtubule-organizing centres 78: 1: 6550:Microtubule severing proteins 4450:10.1016/S0092-8674(00)80560-7 4410:10.1016/S0959-437X(99)80060-4 3935:Knoblich JA (December 2010). 3724:10.1016/s0960-9822(99)80133-x 3299:10.1158/1535-7163.MCT-10-0552 3287:Molecular Cancer Therapeutics 3238:Molecular Biology of the Cell 2522:Molecular Biology of the Cell 2103:Annual Review of Biochemistry 1844:Molecular Biology of the Cell 1731:10.1126/science.177.4054.1104 1419:10.1016/S0092-8674(03)00111-9 1021:Interpolar/Polar microtubules 988:microtubules during mitosis. 978:microtubule organizing center 332:Microtubules are part of the 113:. They provide platforms for 5210:actin depolymerizing factors 4494:10.1016/0165-0173(90)90013-E 3569:10.1016/0896-6273(93)90057-X 3533:10.1016/0955-0674(95)80047-6 2677:10.1016/0092-8674(86)90318-1 2214:10.1371/journal.pbio.1001213 1660:Journal of Molecular Biology 623:Tubulin is also known to be 6688:Plakoglobin (gamma catenin) 4529:The Journal of Cell Biology 3990:The Journal of Cell Biology 3836:The Journal of Cell Biology 2995:The Journal of Cell Biology 1942:The Journal of Cell Biology 61:, as wide as 23 to 27 6990: 2301:10.1038/s41598-017-09832-8 1622:10.1038/s41598-018-37767-1 822: 746: 534:adenomatous polyposis coli 515:"Search and capture" model 412: 404:Microtubule polymerization 328:Intracellular organization 6944: 3599:"The Human Protein Atlas" 2013:10.1016/j.str.2010.05.010 1463:10.1016/j.ceb.2006.12.009 1400:Vale RD (February 2003). 1065:to the site of polarity. 830:identified as a +TIP was 219:and biochemical studies. 6914:Prokaryotic cytoskeleton 931:Some viruses (including 4364:10.1074/jbc.M112.423905 4140:Journal of Cell Science 3795:Genes & Development 3756:Journal of Cell Science 3486:Journal of Cell Science 3453:10.18632/oncotarget.250 3352:10.1074/jbc.M110.160820 3192:10.3390/biology12040561 2770:10.1242/jcs.113.22.3907 2758:Journal of Cell Science 2484:10.1073/pnas.0901587106 2338:Journal of Cell Science 2251:www.merriam-webster.com 2163:10.1073/pnas.0502859102 1893:Journal of Cell Biology 1856:10.1091/mbc.E16-05-0271 1511:10.1073/pnas.1600129113 1327:Journal of Cell Biology 1278:Journal of Cell Biology 1141:epidermal growth factor 1132:Drosophila melanogaster 583:tubulin—tyrosine ligase 281:end-to-end into linear 227:assays for microtubule 115:intracellular transport 4591:10.1074/jbc.M309140200 4541:10.1083/jcb.128.6.1111 4228:10.1093/emboj/18.3.578 1964:10.1083/jcb.107.4.1437 1905:10.1083/jcb.117.5.1031 1672:10.1006/jmbi.2001.5077 1010: 1000:Microtubule subclasses 969: 891: 883: 558: 494: 415:Microtubule nucleation 400: 395:are in green, and the 257: 192:Bacillus thuringiensis 103:intermediate filaments 90: 75:alpha and beta tubulin 49:that form part of the 35: 5534:(hard alpha-keratins) 5365:(soft alpha-keratins) 4617:MBInfo - Microtubules 4002:10.1083/jcb.131.3.721 3848:10.1083/jcb.201612064 3768:10.1242/jcs.110.3.295 3079:Nature Communications 3007:10.1083/jcb.120.3.725 1181:transcription factors 1119:morphogenetic process 1007: 967: 889: 881: 658:programmed cell death 594:: the addition of an 556: 492: 382: 370:endoplasmic reticulum 255: 167:found in most fungi. 87: 33: 6949:cytoskeletal defects 6909:Major sperm proteins 3603:www.proteinatlas.org 3403:10.3390/ijms21051656 2426:10.4161/cc.8.14.9074 1339:10.1083/jcb.82.1.278 1290:10.1083/jcb.19.1.239 671:The cancer-fighting 472:Microtubule dynamics 5362:Epithelial keratins 4304:Nature Cell Biology 4261:Nature Cell Biology 4088:Nature Cell Biology 4039:Nature Cell Biology 3906:10.1038/ncb0305-219 3894:Nature Cell Biology 3715:1999CBio....9.R218M 3498:10.1242/jcs.5.2.433 3250:10.1091/mbc.4.6.615 3136:2002Natur.417..455H 3091:2013NatCo...4.1962K 3052:10.1021/bi00107a022 2848:Nature Cell Biology 2804:Nature Cell Biology 2626:1984Natur.312..237M 2591:10.1021/bi00664a018 2475:2009PNAS..106.6998U 2293:2017NatSR...7.9583Z 2154:2005PNAS..102.9170S 2062:2016NatSR...631723B 1723:1972Sci...177.1104W 1613:2019NatSR...9.3794K 1502:2016PNAS..113E1200J 1244:"Digital Downloads" 1177:signal transduction 1014:Astral microtubules 477:Dynamic instability 217:electron microscope 165:spindle pole bodies 4153:10.1242/jcs.092429 4146:(Pt 12): 2805–14. 3808:10.1101/gad.894001 3100:10.1038/ncomms2962 2344:(Pt 20): 4155–63. 2281:Scientific Reports 2050:Scientific Reports 1601:Scientific Reports 1565:Cooper GM (2000). 1550:2024-02-21 at the 1089:Cilia and flagella 1011: 996:mitosis to occur. 976:is the main MTOC ( 970: 892: 884: 799:CRACD-like protein 787:cytoplasmic dynein 647:A wide variety of 559: 495: 401: 391:are shown in red, 383:Components of the 274:These α/β-tubulin 258: 95:cellular processes 91: 36: 6956: 6955: 6897: 6896: 6657: 6656: 5902: 5901: 5784: 5783: 5327: 5326: 5270: 5269: 3762:(Pt 3): 295–300. 2563:978-0-471-46580-5 2469:(17): 6998–7003. 2351:10.1242/jcs.03227 2070:10.1038/srep31723 1370:Diwan JJ (2006). 1121:of an organism's 611:Polyglutamylation 490: 213:light microscopes 151:and organized by 147:Microtubules are 71:globular proteins 16:(Redirected from 6981: 5918: 5358: 5340: 4701: 4692: 4678: 4656: 4649: 4642: 4633: 4604: 4603: 4593: 4584:(45): 44305–11. 4569: 4563: 4562: 4552: 4520: 4514: 4513: 4477: 4471: 4470: 4452: 4428: 4422: 4421: 4393: 4387: 4386: 4376: 4366: 4357:(52): 43359–69. 4342: 4336: 4335: 4299: 4293: 4292: 4256: 4250: 4249: 4239: 4216:The EMBO Journal 4207: 4201: 4200: 4172: 4166: 4165: 4155: 4131: 4122: 4121: 4111: 4079: 4073: 4072: 4062: 4030: 4024: 4023: 4013: 3981: 3975: 3974: 3964: 3932: 3926: 3925: 3889: 3883: 3876: 3870: 3869: 3859: 3842:(6): 1525–1531. 3827: 3821: 3820: 3810: 3786: 3780: 3779: 3751: 3745: 3744: 3726: 3694: 3688: 3687: 3651: 3645: 3644: 3624: 3618: 3617: 3615: 3614: 3595: 3589: 3588: 3551: 3545: 3544: 3516: 3510: 3509: 3481: 3475: 3474: 3464: 3432: 3426: 3425: 3415: 3405: 3381: 3375: 3374: 3364: 3354: 3345:(42): 32242–50. 3330: 3321: 3320: 3310: 3278: 3272: 3271: 3261: 3229: 3223: 3222: 3212: 3194: 3170: 3164: 3163: 3119: 3113: 3112: 3102: 3070: 3064: 3063: 3035: 3029: 3028: 3018: 2986: 2980: 2979: 2969: 2958:10.1002/cm.21027 2937: 2926: 2925: 2889: 2880: 2879: 2842: 2836: 2835: 2816:10.1038/35087035 2799: 2793: 2792: 2790: 2789: 2749: 2740: 2739: 2703: 2697: 2696: 2660: 2654: 2653: 2634:10.1038/312237a0 2620:(5991): 237–42. 2609: 2603: 2602: 2574: 2568: 2567: 2543: 2537: 2536: 2534: 2533: 2513: 2507: 2506: 2496: 2486: 2454: 2448: 2447: 2437: 2405: 2399: 2398: 2370: 2364: 2363: 2353: 2329: 2323: 2322: 2312: 2272: 2266: 2265: 2263: 2262: 2243: 2237: 2236: 2226: 2216: 2207:(12): e1001213. 2192: 2186: 2185: 2175: 2165: 2133: 2127: 2126: 2098: 2092: 2091: 2081: 2041: 2035: 2034: 2024: 1992: 1986: 1985: 1975: 1957: 1933: 1927: 1926: 1916: 1884: 1878: 1877: 1867: 1835: 1829: 1828: 1792: 1786: 1785: 1757: 1751: 1750: 1717:(4054): 1104–5. 1706: 1695: 1694: 1692: 1691: 1651: 1645: 1644: 1634: 1624: 1592: 1586: 1585: 1583: 1582: 1562: 1556: 1542:Wayne, R. 2009. 1540: 1534: 1533: 1523: 1513: 1481: 1475: 1474: 1446: 1440: 1439: 1421: 1397: 1391: 1390: 1388: 1387: 1378:. Archived from 1367: 1361: 1360: 1350: 1318: 1312: 1311: 1301: 1269: 1263: 1262: 1260: 1259: 1240: 1212: 1207: 1206: 763:τ (tau) proteins 675:class of drugs ( 656:and can lead to 491: 313:Some species of 266:α- and β-tubulin 138:mitotic spindles 21: 6989: 6988: 6984: 6983: 6982: 6980: 6979: 6978: 6959: 6958: 6957: 6952: 6940: 6893: 6796: 6702: 6653: 6566: 6545: 6497: 6320: 6112: 6064: 5910: 5898: 5868: 5815: 5780: 5764: 5648:Ungrouped alpha 5643: 5533: 5525: 5364: 5350: 5344: 5334: 5323: 5266: 5063: 4742: 4684: 4669: 4660: 4613: 4608: 4607: 4571: 4570: 4566: 4522: 4521: 4517: 4479: 4478: 4474: 4430: 4429: 4425: 4395: 4394: 4390: 4344: 4343: 4339: 4316:10.1038/ncb1262 4301: 4300: 4296: 4258: 4257: 4253: 4209: 4208: 4204: 4174: 4173: 4169: 4133: 4132: 4125: 4100:10.1038/ncb1809 4081: 4080: 4076: 4051:10.1038/ncb1890 4032: 4031: 4027: 3983: 3982: 3978: 3953:10.1038/nrm3010 3934: 3933: 3929: 3891: 3890: 3886: 3877: 3873: 3829: 3828: 3824: 3801:(10): 1167–81. 3788: 3787: 3783: 3753: 3752: 3748: 3703:Current Biology 3696: 3695: 3691: 3668:10.1038/nrm2774 3653: 3652: 3648: 3626: 3625: 3621: 3612: 3610: 3597: 3596: 3592: 3553: 3552: 3548: 3518: 3517: 3513: 3483: 3482: 3478: 3434: 3433: 3429: 3383: 3382: 3378: 3332: 3331: 3324: 3293:(11): 2914–23. 3280: 3279: 3275: 3231: 3230: 3226: 3172: 3171: 3167: 3144:10.1038/417455a 3130:(6887): 455–8. 3121: 3120: 3116: 3072: 3071: 3067: 3046:(43): 10523–8. 3037: 3036: 3032: 2988: 2987: 2983: 2939: 2938: 2929: 2906:10.1038/nrm3227 2891: 2890: 2883: 2860:10.1038/ncb1160 2844: 2843: 2839: 2801: 2800: 2796: 2787: 2785: 2764:(22): 3907–19. 2751: 2750: 2743: 2720:10.1038/nrm2310 2705: 2704: 2700: 2662: 2661: 2657: 2611: 2610: 2606: 2585:(19): 4248–54. 2576: 2575: 2571: 2564: 2546:Karp G (2005). 2545: 2544: 2540: 2531: 2529: 2515: 2514: 2510: 2456: 2455: 2451: 2420:(14): 2168–74. 2407: 2406: 2402: 2372: 2371: 2367: 2331: 2330: 2326: 2274: 2273: 2269: 2260: 2258: 2245: 2244: 2240: 2194: 2193: 2189: 2135: 2134: 2130: 2100: 2099: 2095: 2043: 2042: 2038: 1994: 1993: 1989: 1935: 1934: 1930: 1886: 1885: 1881: 1850:(22): 2924–31. 1837: 1836: 1832: 1794: 1793: 1789: 1759: 1758: 1754: 1708: 1707: 1698: 1689: 1687: 1653: 1652: 1648: 1594: 1593: 1589: 1580: 1578: 1564: 1563: 1559: 1552:Wayback Machine 1541: 1537: 1483: 1482: 1478: 1448: 1447: 1443: 1399: 1398: 1394: 1385: 1383: 1369: 1368: 1364: 1320: 1319: 1315: 1271: 1270: 1266: 1257: 1255: 1242: 1241: 1237: 1232: 1208: 1201: 1198: 1173:gene expression 1168: 1166:Gene regulation 1115: 1091: 1051: 1046: 1037: 1002: 962: 957: 876: 827: 821: 751: 745: 740: 645: 617:Polyglycylation 585:(TTL) is known. 551: 546: 517: 481: 479: 474: 465: 448:Golgi apparatus 417: 411: 406: 389:Actin filaments 374:Golgi apparatus 330: 316:Prosthecobacter 302:organisms like 250: 205: 28: 23: 22: 15: 12: 11: 5: 6987: 6985: 6977: 6976: 6971: 6961: 6960: 6954: 6953: 6945: 6942: 6941: 6939: 6938: 6937: 6936: 6931: 6926: 6921: 6911: 6905: 6903: 6899: 6898: 6895: 6894: 6892: 6891: 6886: 6881: 6880: 6879: 6874: 6864: 6859: 6858: 6857: 6847: 6846: 6845: 6840: 6835: 6830: 6825: 6820: 6815: 6813:Corneodesmosin 6804: 6802: 6798: 6797: 6795: 6794: 6793: 6792: 6787: 6782: 6777: 6772: 6767: 6762: 6752: 6751: 6750: 6745: 6740: 6730: 6725: 6724: 6723: 6712: 6710: 6704: 6703: 6701: 6700: 6695: 6690: 6685: 6684: 6683: 6673: 6667: 6665: 6659: 6658: 6655: 6654: 6652: 6651: 6650: 6649: 6644: 6639: 6629: 6628: 6627: 6622: 6617: 6612: 6607: 6597: 6592: 6591: 6590: 6580: 6574: 6572: 6568: 6567: 6565: 6564: 6559: 6553: 6551: 6547: 6546: 6544: 6543: 6538: 6533: 6528: 6523: 6518: 6513: 6507: 6505: 6499: 6498: 6496: 6495: 6490: 6485: 6480: 6475: 6470: 6465: 6460: 6455: 6450: 6445: 6440: 6435: 6428: 6427: 6422: 6417: 6412: 6407: 6402: 6397: 6392: 6387: 6382: 6377: 6372: 6367: 6362: 6357: 6352: 6347: 6342: 6337: 6330: 6328: 6322: 6321: 6319: 6318: 6313: 6308: 6303: 6298: 6293: 6288: 6283: 6278: 6273: 6268: 6263: 6258: 6253: 6248: 6243: 6238: 6233: 6228: 6223: 6218: 6213: 6208: 6203: 6198: 6193: 6188: 6183: 6178: 6173: 6168: 6163: 6158: 6153: 6148: 6143: 6138: 6133: 6128: 6122: 6120: 6114: 6113: 6111: 6110: 6105: 6100: 6095: 6090: 6085: 6080: 6074: 6072: 6066: 6065: 6063: 6062: 6057: 6052: 6047: 6042: 6037: 6032: 6027: 6022: 6017: 6012: 6007: 6002: 5997: 5992: 5987: 5982: 5977: 5972: 5967: 5962: 5957: 5952: 5947: 5942: 5937: 5932: 5926: 5924: 5915: 5904: 5903: 5900: 5899: 5897: 5896: 5891: 5886: 5880:Nuclear lamins 5876: 5874: 5870: 5869: 5867: 5866: 5861: 5856: 5855: 5854: 5849: 5844: 5834: 5829: 5823: 5821: 5817: 5816: 5814: 5813: 5808: 5803: 5798: 5792: 5790: 5786: 5785: 5782: 5781: 5779: 5778: 5772: 5770: 5766: 5765: 5763: 5762: 5761: 5760: 5755: 5750: 5745: 5740: 5735: 5730: 5725: 5720: 5715: 5702: 5701: 5700: 5699: 5694: 5689: 5684: 5679: 5674: 5669: 5664: 5651: 5649: 5645: 5644: 5642: 5641: 5640: 5639: 5634: 5629: 5624: 5619: 5614: 5597: 5596: 5595: 5594: 5589: 5584: 5579: 5574: 5569: 5564: 5559: 5554: 5537: 5535: 5527: 5526: 5524: 5523: 5522: 5521: 5516: 5511: 5506: 5501: 5496: 5491: 5486: 5481: 5476: 5459: 5458: 5457: 5456: 5446: 5445: 5444: 5432: 5431: 5430: 5425: 5420: 5415: 5410: 5405: 5400: 5395: 5390: 5385: 5368: 5366: 5355: 5337: 5329: 5328: 5325: 5324: 5322: 5321: 5316: 5311: 5310: 5309: 5304: 5299: 5289: 5284: 5278: 5276: 5272: 5271: 5268: 5267: 5265: 5264: 5259: 5258: 5257: 5252: 5242: 5237: 5236: 5235: 5230: 5229: 5228: 5223: 5206: 5204:Arp2/3 complex 5201: 5200: 5199: 5194: 5189: 5184: 5173: 5172: 5171: 5170: 5165: 5160: 5155: 5145: 5144: 5143: 5129: 5118: 5099: 5098: 5097: 5092: 5087: 5082: 5071: 5069: 5065: 5064: 5062: 5061: 5060: 5059: 5054: 5049: 5044: 5039: 5034: 5029: 5024: 5019: 5014: 5009: 5004: 4999: 4989: 4988: 4987: 4982: 4974: 4973: 4972: 4964: 4963: 4962: 4954: 4953: 4952: 4947: 4939: 4938: 4937: 4932: 4924: 4923: 4922: 4914: 4913: 4912: 4907: 4902: 4894: 4893: 4892: 4887: 4879: 4878: 4877: 4872: 4867: 4862: 4857: 4852: 4847: 4842: 4837: 4832: 4827: 4822: 4817: 4812: 4807: 4799: 4798: 4797: 4791: 4786: 4781: 4776: 4771: 4766: 4761: 4752: 4750: 4744: 4743: 4741: 4740: 4735: 4730: 4725: 4720: 4715: 4709: 4707: 4698: 4689: 4682:Microfilaments 4675: 4671: 4670: 4661: 4659: 4658: 4651: 4644: 4636: 4630: 4629: 4624: 4619: 4612: 4611:External links 4609: 4606: 4605: 4564: 4515: 4472: 4443:(2): 195–209. 4423: 4404:(4): 396–404. 4388: 4337: 4294: 4251: 4202: 4167: 4123: 4074: 4025: 3976: 3947:(12): 849–60. 3927: 3884: 3871: 3822: 3781: 3746: 3709:(6): R218–20. 3689: 3662:(10): 682–96. 3646: 3619: 3590: 3563:(6): 1089–99. 3546: 3511: 3476: 3447:(5): 368–377. 3427: 3376: 3322: 3273: 3224: 3165: 3114: 3065: 3030: 2981: 2927: 2900:(12): 773–86. 2881: 2837: 2794: 2741: 2698: 2655: 2604: 2569: 2562: 2538: 2508: 2449: 2400: 2365: 2324: 2267: 2238: 2187: 2148:(26): 9170–5. 2128: 2093: 2036: 2007:(8): 1022–31. 1987: 1955:10.1.1.525.507 1948:(4): 1437–48. 1928: 1899:(5): 1031–40. 1879: 1830: 1787: 1752: 1696: 1666:(5): 1045–57. 1646: 1587: 1557: 1535: 1496:(9): E1200-5. 1476: 1441: 1392: 1372:"Microtubules" 1362: 1313: 1264: 1234: 1233: 1231: 1228: 1227: 1226: 1220: 1214: 1213: 1210:Biology portal 1197: 1194: 1186:growth factors 1167: 1164: 1160:nervous system 1114: 1111: 1090: 1087: 1082:focal adhesion 1050: 1049:Cell migration 1047: 1045: 1042: 1036: 1033: 1001: 998: 961: 958: 956: 953: 949:motor proteins 929: 928: 921: 875: 874:Motor proteins 872: 823:Main article: 820: 817: 747:Main article: 744: 741: 739: 736: 723: 722: 716: 701: 685: 684: 644: 641: 625:phosphorylated 621: 620: 614: 608: 589: 586: 571:Detyrosination 550: 547: 545: 542: 521:Marc Kirschner 516: 513: 478: 475: 473: 470: 464: 463:Polymerization 461: 456:trypanosomatid 413:Main article: 410: 407: 405: 402: 387:cytoskeleton. 329: 326: 320:both α- and β- 283:protofilaments 249: 246: 229:motor proteins 204: 201: 172:motor proteins 155:, such as the 99:microfilaments 79:protofilaments 26: 24: 14: 13: 10: 9: 6: 4: 3: 2: 6986: 6975: 6972: 6970: 6967: 6966: 6964: 6951: 6950: 6943: 6935: 6932: 6930: 6927: 6925: 6922: 6920: 6917: 6916: 6915: 6912: 6910: 6907: 6906: 6904: 6900: 6890: 6887: 6885: 6882: 6878: 6875: 6873: 6870: 6869: 6868: 6865: 6863: 6860: 6856: 6853: 6852: 6851: 6848: 6844: 6841: 6839: 6836: 6834: 6831: 6829: 6826: 6824: 6821: 6819: 6816: 6814: 6811: 6810: 6809: 6806: 6805: 6803: 6799: 6791: 6788: 6786: 6783: 6781: 6778: 6776: 6773: 6771: 6768: 6766: 6763: 6761: 6758: 6757: 6756: 6753: 6749: 6746: 6744: 6741: 6739: 6736: 6735: 6734: 6731: 6729: 6726: 6722: 6719: 6718: 6717: 6714: 6713: 6711: 6709: 6705: 6699: 6696: 6694: 6693:Delta catenin 6691: 6689: 6686: 6682: 6679: 6678: 6677: 6674: 6672: 6671:Alpha catenin 6669: 6668: 6666: 6664: 6660: 6648: 6645: 6643: 6640: 6638: 6635: 6634: 6633: 6630: 6626: 6623: 6621: 6618: 6616: 6613: 6611: 6608: 6606: 6603: 6602: 6601: 6598: 6596: 6593: 6589: 6586: 6585: 6584: 6581: 6579: 6576: 6575: 6573: 6569: 6563: 6560: 6558: 6555: 6554: 6552: 6548: 6542: 6539: 6537: 6534: 6532: 6529: 6527: 6524: 6522: 6519: 6517: 6514: 6512: 6509: 6508: 6506: 6504: 6500: 6494: 6491: 6489: 6486: 6484: 6481: 6479: 6476: 6474: 6471: 6469: 6466: 6464: 6461: 6459: 6456: 6454: 6451: 6449: 6446: 6444: 6441: 6439: 6436: 6434: 6431:cytoplasmic: 6430: 6429: 6426: 6423: 6421: 6418: 6416: 6413: 6411: 6408: 6406: 6403: 6401: 6398: 6396: 6393: 6391: 6388: 6386: 6383: 6381: 6378: 6376: 6373: 6371: 6368: 6366: 6363: 6361: 6358: 6356: 6353: 6351: 6348: 6346: 6343: 6341: 6338: 6336: 6332: 6331: 6329: 6327: 6323: 6317: 6314: 6312: 6309: 6307: 6304: 6302: 6299: 6297: 6294: 6292: 6289: 6287: 6284: 6282: 6279: 6277: 6274: 6272: 6269: 6267: 6264: 6262: 6259: 6257: 6254: 6252: 6249: 6247: 6244: 6242: 6239: 6237: 6234: 6232: 6229: 6227: 6224: 6222: 6219: 6217: 6214: 6212: 6209: 6207: 6204: 6202: 6199: 6197: 6194: 6192: 6189: 6187: 6184: 6182: 6179: 6177: 6174: 6172: 6169: 6167: 6164: 6162: 6159: 6157: 6154: 6152: 6149: 6147: 6144: 6142: 6139: 6137: 6134: 6132: 6129: 6127: 6124: 6123: 6121: 6119: 6115: 6109: 6106: 6104: 6101: 6099: 6096: 6094: 6091: 6089: 6086: 6084: 6081: 6079: 6076: 6075: 6073: 6071: 6067: 6061: 6058: 6056: 6053: 6051: 6048: 6046: 6043: 6041: 6038: 6036: 6033: 6031: 6028: 6026: 6023: 6021: 6018: 6016: 6013: 6011: 6008: 6006: 6003: 6001: 5998: 5996: 5993: 5991: 5988: 5986: 5983: 5981: 5978: 5976: 5973: 5971: 5968: 5966: 5963: 5961: 5958: 5956: 5953: 5951: 5948: 5946: 5943: 5941: 5938: 5936: 5933: 5931: 5928: 5927: 5925: 5923: 5919: 5916: 5914: 5909: 5905: 5895: 5892: 5890: 5887: 5885: 5881: 5878: 5877: 5875: 5871: 5865: 5862: 5860: 5857: 5853: 5850: 5848: 5845: 5843: 5840: 5839: 5838: 5837:Neurofilament 5835: 5833: 5830: 5828: 5825: 5824: 5822: 5818: 5812: 5809: 5807: 5804: 5802: 5799: 5797: 5794: 5793: 5791: 5787: 5777: 5774: 5773: 5771: 5767: 5759: 5756: 5754: 5751: 5749: 5746: 5744: 5741: 5739: 5736: 5734: 5731: 5729: 5726: 5724: 5721: 5719: 5716: 5714: 5711: 5710: 5709: 5708: 5707:chromosome 12 5704: 5703: 5698: 5695: 5693: 5690: 5688: 5685: 5683: 5680: 5678: 5675: 5673: 5670: 5668: 5665: 5663: 5660: 5659: 5658: 5657: 5656:chromosome 17 5653: 5652: 5650: 5646: 5638: 5635: 5633: 5630: 5628: 5625: 5623: 5620: 5618: 5615: 5613: 5610: 5609: 5608: 5607: 5606:chromosome 12 5603: 5599: 5598: 5593: 5590: 5588: 5585: 5583: 5580: 5578: 5575: 5573: 5570: 5568: 5565: 5563: 5560: 5558: 5555: 5553: 5550: 5549: 5548: 5547: 5546:chromosome 17 5543: 5539: 5538: 5536: 5532: 5531:Hair keratins 5528: 5520: 5517: 5515: 5512: 5510: 5507: 5505: 5502: 5500: 5497: 5495: 5492: 5490: 5487: 5485: 5482: 5480: 5477: 5475: 5472: 5471: 5470: 5469: 5468:chromosome 12 5465: 5461: 5460: 5455: 5452: 5451: 5450: 5447: 5443: 5440: 5439: 5438: 5437: 5436:chromosome 12 5433: 5429: 5426: 5424: 5421: 5419: 5416: 5414: 5411: 5409: 5406: 5404: 5401: 5399: 5396: 5394: 5391: 5389: 5386: 5384: 5381: 5380: 5379: 5378: 5377:chromosome 17 5374: 5370: 5369: 5367: 5363: 5359: 5356: 5353: 5348: 5341: 5338: 5336: 5333:Intermediate 5330: 5320: 5317: 5315: 5312: 5308: 5305: 5303: 5300: 5298: 5295: 5294: 5293: 5290: 5288: 5285: 5283: 5280: 5279: 5277: 5273: 5263: 5260: 5256: 5253: 5251: 5248: 5247: 5246: 5243: 5241: 5238: 5234: 5231: 5227: 5224: 5222: 5219: 5218: 5217: 5214: 5213: 5212: 5211: 5207: 5205: 5202: 5198: 5195: 5193: 5190: 5188: 5185: 5183: 5180: 5179: 5178: 5175: 5174: 5169: 5166: 5164: 5161: 5159: 5156: 5154: 5151: 5150: 5149: 5146: 5142: 5139: 5136: 5133: 5130: 5128: 5125: 5122: 5119: 5117: 5114: 5111: 5108: 5105: 5104: 5103: 5100: 5096: 5093: 5091: 5088: 5086: 5083: 5081: 5078: 5077: 5076: 5073: 5072: 5070: 5066: 5058: 5055: 5053: 5050: 5048: 5045: 5043: 5040: 5038: 5035: 5033: 5030: 5028: 5025: 5023: 5020: 5018: 5015: 5013: 5010: 5008: 5005: 5003: 5000: 4998: 4995: 4994: 4993: 4990: 4986: 4983: 4981: 4978: 4977: 4975: 4971: 4968: 4967: 4965: 4961: 4958: 4957: 4955: 4951: 4948: 4946: 4943: 4942: 4940: 4936: 4933: 4931: 4928: 4927: 4925: 4921: 4918: 4917: 4915: 4911: 4908: 4906: 4903: 4901: 4898: 4897: 4895: 4891: 4888: 4886: 4883: 4882: 4880: 4876: 4873: 4871: 4868: 4866: 4863: 4861: 4858: 4856: 4853: 4851: 4848: 4846: 4843: 4841: 4838: 4836: 4833: 4831: 4828: 4826: 4823: 4821: 4818: 4816: 4813: 4811: 4808: 4806: 4803: 4802: 4800: 4795: 4792: 4790: 4787: 4785: 4782: 4780: 4777: 4775: 4772: 4770: 4767: 4765: 4762: 4760: 4757: 4756: 4754: 4753: 4751: 4749: 4745: 4739: 4736: 4734: 4731: 4729: 4726: 4724: 4721: 4719: 4716: 4714: 4711: 4710: 4708: 4706: 4702: 4699: 4697: 4693: 4690: 4688: 4683: 4679: 4676: 4672: 4668: 4664: 4657: 4652: 4650: 4645: 4643: 4638: 4637: 4634: 4628: 4625: 4623: 4620: 4618: 4615: 4614: 4610: 4601: 4597: 4592: 4587: 4583: 4579: 4575: 4568: 4565: 4560: 4556: 4551: 4546: 4542: 4538: 4535:(6): 1111–9. 4534: 4530: 4526: 4519: 4516: 4511: 4507: 4503: 4499: 4495: 4491: 4488:(2): 101–20. 4487: 4483: 4476: 4473: 4468: 4464: 4460: 4456: 4451: 4446: 4442: 4438: 4434: 4427: 4424: 4419: 4415: 4411: 4407: 4403: 4399: 4392: 4389: 4384: 4380: 4375: 4370: 4365: 4360: 4356: 4352: 4348: 4341: 4338: 4333: 4329: 4325: 4321: 4317: 4313: 4310:(6): 581–90. 4309: 4305: 4298: 4295: 4290: 4286: 4282: 4278: 4274: 4270: 4266: 4262: 4255: 4252: 4247: 4243: 4238: 4233: 4229: 4225: 4222:(3): 578–85. 4221: 4217: 4213: 4206: 4203: 4198: 4194: 4190: 4186: 4183:(4): 325–40. 4182: 4178: 4171: 4168: 4163: 4159: 4154: 4149: 4145: 4141: 4137: 4130: 4128: 4124: 4119: 4115: 4110: 4105: 4101: 4097: 4093: 4089: 4085: 4078: 4075: 4070: 4066: 4061: 4056: 4052: 4048: 4044: 4040: 4036: 4029: 4026: 4021: 4017: 4012: 4007: 4003: 3999: 3996:(3): 721–34. 3995: 3991: 3987: 3980: 3977: 3972: 3968: 3963: 3958: 3954: 3950: 3946: 3942: 3938: 3931: 3928: 3923: 3919: 3915: 3911: 3907: 3903: 3900:(3): 219–22. 3899: 3895: 3888: 3885: 3881: 3875: 3872: 3867: 3863: 3858: 3853: 3849: 3845: 3841: 3837: 3833: 3826: 3823: 3818: 3814: 3809: 3804: 3800: 3796: 3792: 3785: 3782: 3777: 3773: 3769: 3765: 3761: 3757: 3750: 3747: 3742: 3738: 3734: 3730: 3725: 3720: 3716: 3712: 3708: 3704: 3700: 3693: 3690: 3685: 3681: 3677: 3673: 3669: 3665: 3661: 3657: 3650: 3647: 3642: 3638: 3634: 3630: 3623: 3620: 3608: 3604: 3600: 3594: 3591: 3586: 3582: 3578: 3574: 3570: 3566: 3562: 3558: 3550: 3547: 3542: 3538: 3534: 3530: 3526: 3522: 3515: 3512: 3507: 3503: 3499: 3495: 3492:(2): 433–51. 3491: 3487: 3480: 3477: 3472: 3468: 3463: 3458: 3454: 3450: 3446: 3442: 3438: 3431: 3428: 3423: 3419: 3414: 3409: 3404: 3399: 3395: 3391: 3387: 3380: 3377: 3372: 3368: 3363: 3358: 3353: 3348: 3344: 3340: 3336: 3329: 3327: 3323: 3318: 3314: 3309: 3304: 3300: 3296: 3292: 3288: 3284: 3277: 3274: 3269: 3265: 3260: 3255: 3251: 3247: 3244:(6): 615–26. 3243: 3239: 3235: 3228: 3225: 3220: 3216: 3211: 3206: 3202: 3198: 3193: 3188: 3184: 3180: 3176: 3169: 3166: 3161: 3157: 3153: 3149: 3145: 3141: 3137: 3133: 3129: 3125: 3118: 3115: 3110: 3106: 3101: 3096: 3092: 3088: 3084: 3080: 3076: 3069: 3066: 3061: 3057: 3053: 3049: 3045: 3041: 3034: 3031: 3026: 3022: 3017: 3012: 3008: 3004: 3001:(3): 725–32. 3000: 2996: 2992: 2985: 2982: 2977: 2973: 2968: 2963: 2959: 2955: 2952:(7): 442–63. 2951: 2947: 2943: 2936: 2934: 2932: 2928: 2923: 2919: 2915: 2911: 2907: 2903: 2899: 2895: 2888: 2886: 2882: 2877: 2873: 2869: 2865: 2861: 2857: 2854:(9): 820–30. 2853: 2849: 2841: 2838: 2833: 2829: 2825: 2821: 2817: 2813: 2809: 2805: 2798: 2795: 2783: 2779: 2775: 2771: 2767: 2763: 2759: 2755: 2748: 2746: 2742: 2737: 2733: 2729: 2725: 2721: 2717: 2713: 2709: 2702: 2699: 2694: 2690: 2686: 2682: 2678: 2674: 2671:(3): 329–42. 2670: 2666: 2659: 2656: 2651: 2647: 2643: 2639: 2635: 2631: 2627: 2623: 2619: 2615: 2608: 2605: 2600: 2596: 2592: 2588: 2584: 2580: 2573: 2570: 2565: 2559: 2555: 2551: 2550: 2542: 2539: 2527: 2523: 2519: 2512: 2509: 2504: 2500: 2495: 2490: 2485: 2480: 2476: 2472: 2468: 2464: 2460: 2453: 2450: 2445: 2441: 2436: 2431: 2427: 2423: 2419: 2415: 2411: 2404: 2401: 2396: 2392: 2388: 2384: 2380: 2376: 2369: 2366: 2361: 2357: 2352: 2347: 2343: 2339: 2335: 2328: 2325: 2320: 2316: 2311: 2306: 2302: 2298: 2294: 2290: 2286: 2282: 2278: 2271: 2268: 2256: 2252: 2248: 2242: 2239: 2234: 2230: 2225: 2220: 2215: 2210: 2206: 2202: 2198: 2191: 2188: 2183: 2179: 2174: 2169: 2164: 2159: 2155: 2151: 2147: 2143: 2139: 2132: 2129: 2124: 2120: 2116: 2112: 2108: 2104: 2097: 2094: 2089: 2085: 2080: 2075: 2071: 2067: 2063: 2059: 2055: 2051: 2047: 2040: 2037: 2032: 2028: 2023: 2018: 2014: 2010: 2006: 2002: 1998: 1991: 1988: 1983: 1979: 1974: 1969: 1965: 1961: 1956: 1951: 1947: 1943: 1939: 1932: 1929: 1924: 1920: 1915: 1910: 1906: 1902: 1898: 1894: 1890: 1883: 1880: 1875: 1871: 1866: 1861: 1857: 1853: 1849: 1845: 1841: 1834: 1831: 1826: 1822: 1818: 1814: 1810: 1806: 1802: 1798: 1791: 1788: 1783: 1779: 1775: 1771: 1767: 1763: 1756: 1753: 1748: 1744: 1740: 1736: 1732: 1728: 1724: 1720: 1716: 1712: 1705: 1703: 1701: 1697: 1685: 1681: 1677: 1673: 1669: 1665: 1661: 1657: 1650: 1647: 1642: 1638: 1633: 1628: 1623: 1618: 1614: 1610: 1606: 1602: 1598: 1591: 1588: 1576: 1572: 1568: 1561: 1558: 1554: 1553: 1549: 1546: 1539: 1536: 1531: 1527: 1522: 1517: 1512: 1507: 1503: 1499: 1495: 1491: 1487: 1480: 1477: 1472: 1468: 1464: 1460: 1456: 1452: 1445: 1442: 1437: 1433: 1429: 1425: 1420: 1415: 1412:(4): 467–80. 1411: 1407: 1403: 1396: 1393: 1382:on 2014-02-06 1381: 1377: 1373: 1366: 1363: 1358: 1354: 1349: 1344: 1340: 1336: 1333:(1): 278–89. 1332: 1328: 1324: 1317: 1314: 1309: 1305: 1300: 1295: 1291: 1287: 1284:(1): 239–50. 1283: 1279: 1275: 1268: 1265: 1253: 1249: 1245: 1239: 1236: 1229: 1224: 1221: 1219: 1218:Microtentacle 1216: 1215: 1211: 1205: 1200: 1195: 1193: 1191: 1187: 1182: 1178: 1174: 1165: 1163: 1161: 1157: 1153: 1148: 1146: 1142: 1138: 1137:embryogenesis 1134: 1133: 1128: 1124: 1120: 1112: 1110: 1108: 1104: 1100: 1096: 1088: 1086: 1083: 1079: 1075: 1071: 1066: 1064: 1060: 1056: 1048: 1043: 1041: 1034: 1032: 1029: 1025: 1022: 1018: 1015: 1006: 999: 997: 993: 989: 985: 983: 979: 975: 966: 959: 954: 952: 950: 946: 942: 938: 937:herpesviruses 934: 925: 922: 919: 914: 909: 906: 905: 904: 902: 898: 888: 880: 873: 871: 869: 865: 861: 857: 853: 849: 845: 841: 837: 833: 826: 818: 816: 815: 811: 807: 802: 800: 796: 792: 788: 784: 780: 776: 772: 768: 764: 760: 756: 750: 742: 737: 735: 733: 727: 720: 717: 714: 710: 706: 703:Vinorelbine, 702: 699: 695: 691: 690: 689: 682: 678: 674: 670: 669: 668: 665: 663: 659: 655: 650: 642: 640: 638: 637:palmitoylated 634: 630: 629:ubiquitinated 626: 618: 615: 612: 609: 606: 602: 597: 593: 590: 587: 584: 580: 576: 572: 569: 568: 567: 564: 555: 548: 543: 541: 539: 536:protein, and 535: 531: 526: 525:Tim Mitchison 522: 514: 512: 509: 505: 501: 476: 471: 469: 462: 460: 457: 452: 449: 445: 441: 437: 433: 428: 426: 422: 416: 408: 403: 398: 394: 390: 386: 381: 377: 375: 371: 366: 362: 358: 354: 349: 347: 343: 339: 335: 327: 325: 323: 318: 317: 311: 307: 305: 301: 295: 291: 289: 284: 280: 277: 272: 270: 267: 263: 254: 247: 245: 243: 238: 234: 230: 226: 225: 220: 218: 214: 210: 202: 200: 198: 194: 193: 188: 187:gram-positive 184: 180: 176: 173: 168: 166: 162: 158: 154: 150: 145: 143: 139: 135: 131: 127: 123: 120: 116: 112: 108: 104: 100: 96: 86: 82: 80: 76: 72: 68: 64: 60: 56: 52: 48: 44: 40: 32: 19: 6974:Cytoskeleton 6969:Cell anatomy 6946: 6721:Dystroglycan 6676:Beta catenin 5908:Microtubules 5907: 5776:Beta-keratin 5705: 5654: 5600: 5540: 5462: 5448: 5434: 5371: 5208: 5075:Tropomodulin 4667:cytoskeleton 4581: 4577: 4567: 4532: 4528: 4518: 4485: 4481: 4475: 4440: 4436: 4426: 4401: 4397: 4391: 4354: 4350: 4340: 4307: 4303: 4297: 4273:10.1038/9018 4267:(1): 45–50. 4264: 4260: 4254: 4219: 4215: 4205: 4180: 4176: 4170: 4143: 4139: 4094:(1): 27–35. 4091: 4087: 4077: 4045:(7): 832–8. 4042: 4038: 4028: 3993: 3989: 3979: 3944: 3940: 3930: 3897: 3893: 3887: 3879: 3874: 3839: 3835: 3825: 3798: 3794: 3784: 3759: 3755: 3749: 3706: 3702: 3692: 3659: 3655: 3649: 3632: 3628: 3622: 3611:. Retrieved 3602: 3593: 3560: 3556: 3549: 3527:(1): 72–81. 3524: 3520: 3514: 3489: 3485: 3479: 3444: 3440: 3430: 3393: 3389: 3379: 3342: 3338: 3290: 3286: 3276: 3241: 3237: 3227: 3182: 3178: 3168: 3127: 3123: 3117: 3082: 3078: 3068: 3043: 3040:Biochemistry 3039: 3033: 2998: 2994: 2984: 2949: 2946:Cytoskeleton 2945: 2897: 2893: 2851: 2847: 2840: 2810:(8): 723–9. 2807: 2803: 2797: 2786:. Retrieved 2761: 2757: 2714:(1): 33–46. 2711: 2707: 2701: 2668: 2664: 2658: 2617: 2613: 2607: 2582: 2579:Biochemistry 2578: 2572: 2548: 2541: 2530:. Retrieved 2521: 2511: 2466: 2462: 2452: 2417: 2413: 2403: 2378: 2374: 2368: 2341: 2337: 2327: 2284: 2280: 2270: 2259:. Retrieved 2250: 2241: 2204: 2201:PLOS Biology 2200: 2190: 2145: 2141: 2131: 2106: 2102: 2096: 2053: 2049: 2039: 2004: 2000: 1990: 1945: 1941: 1931: 1896: 1892: 1882: 1847: 1843: 1833: 1800: 1796: 1790: 1765: 1761: 1755: 1714: 1710: 1688:. Retrieved 1663: 1659: 1649: 1604: 1600: 1590: 1579:. Retrieved 1570: 1560: 1543: 1538: 1493: 1489: 1479: 1454: 1450: 1444: 1409: 1405: 1395: 1384:. Retrieved 1380:the original 1375: 1365: 1330: 1326: 1316: 1281: 1277: 1267: 1256:. Retrieved 1248:PurSolutions 1247: 1238: 1169: 1149: 1130: 1116: 1092: 1067: 1052: 1038: 1027: 1026: 1020: 1019: 1013: 1012: 994: 990: 986: 971: 945:adenoviruses 941:parvoviruses 933:retroviruses 930: 893: 828: 803: 773:, MAP-3 and 766: 754: 752: 728: 724: 686: 679:(taxol) and 666: 646: 622: 560: 518: 496: 466: 453: 444:basal bodies 429: 418: 393:microtubules 350: 342:neurotubules 334:cytoskeleton 331: 314: 312: 308: 304:foraminifera 296: 292: 287: 282: 273: 259: 222: 221: 206: 190: 169: 161:basal bodies 146: 92: 89:microtubule. 51:cytoskeleton 39:Microtubules 38: 37: 18:Microtubules 6867:Plakophilin 6818:Desmoplakin 6578:Tau protein 5352:Cytokeratin 5148:Tropomyosin 4696:Myofilament 3880:Curr. Biol. 3635:: 117–143. 3396:(5): 1656. 2287:(1): 9583. 2109:: 277–302. 1607:(1): 3794. 1457:(1): 31–5. 1156:vertebrates 1135:during its 1123:development 1113:Development 1103:Prokaryotes 1059:fibroblasts 960:Centrosomes 732:heavy water 709:vincristine 698:Ixabepilone 694:epothilones 592:Acetylation 365:fibroblasts 209:Leeuwenhoek 142:chromosomes 59:micrometres 6963:Categories 6947:See also: 6919:Crescentin 6838:Periplakin 6828:Envoplakin 6716:Dystrophin 6333:axonemal: 5827:Internexin 5806:Peripherin 3613:2017-04-27 3441:Oncotarget 3185:(4): 561. 2788:2014-06-23 2532:2017-09-05 2414:Cell Cycle 2381:: 83–117. 2261:2018-09-26 1803:: 83–117. 1768:: 83–117. 1690:2019-09-09 1581:2019-03-12 1386:2014-02-24 1258:2020-02-20 1230:References 1154:in higher 1070:G-proteins 1055:interphase 982:centrioles 974:centrosome 713:colchicine 705:Nocodazole 677:paclitaxel 654:cell cycle 633:sumoylated 504:hydrolyzed 432:centrosome 409:Nucleation 385:eukaryotic 279:polymerize 262:eukaryotes 189:bacterium 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