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Myristoylation

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are commonly coupled modifications. Myristoylation alone can promote transient membrane interactions that enable proteins to anchor to membranes but dissociate easily. Further palmitoylation allows for tighter anchoring and slower dissociation from membranes when required by the cell. This specific
324: 713:. Apoptosis can proceed by either mitochondrial or receptor mediated activation. In receptor mediated apoptosis, apoptotic pathways are triggered when the cell binds a death receptor. In one such case, death receptor binding initiates the formation of the 1531:
Doll, Sebastian; Freitas, Florencio Porto; Shah, Ron; Aldrovandi, Maceler; da Silva, Milene Costa; Ingold, Irina; Goya Grocin, Andrea; Xavier da Silva, Thamara Nishida; Panzilius, Elena; Scheel, Christina H.; Mourão, André (November 2019).
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in the cell. Once GTP is bound to the myristoylated protein, it becomes activated, exposing the myristoyl group. These conformational switches can be utilized as a signal for cellular localization, membrane-protein, and
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regions of the protein rather than solvent exposed. By regulating the orientation of the myristoyl group, these processes can be highly coordinated and closely controlled. Myristoylation is thus a form of
842:, is myristoylated. This myristoylation modification targets gag to the membrane of the host cell. Utilizing the myristoyl-electrostatic switch, including a basic patch on the matrix protein, 594:
Both hydrophobic myristoyl groups and "basic patches" (highly positive regions on the protein) characterize myristoyl-electrostatic switches. The basic patch allows for favorable
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of the Îł subunit, and myristoylation is involved in tethering the G protein to the inner surface of the plasma membrane so that the G protein can interact with its receptor.
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Co-translational and post-translational covalent modifications enable proteins to develop higher levels of complexity in cellular function, further adding diversity to the
1132:"Inhibitory monoclonal antibody against a (myristylated) small-molecular-weight antigen from Plasmodium falciparum associated with the parasitophorous vacuole membrane" 1517: 1039: 574:
Myristoylation not only diversifies the function of a protein, but also adds layers of regulation to it. One of the most common functions of the myristoyl group is in
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in the protein, resulting in exposure of the myristoyl group. Similarly, some myristoylated proteins are activated not by a designated ligand, but by the exchange of
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of nearby residues. Additional phosphorylation of the same protein can decrease the electrostatic affinity of the myristoylated protein for the membrane, causing
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that relies on myristoylation of one of its structural proteins in order to successfully package its genome, assemble and mature into a new infectious particle.
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Positive (basic) residues on the protein interact with negatively charged phospholipids on the membrane stabilizing myristoyl-dependent membrane association.
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Levental, Ilya; Grzybek, Michal; Simons, Kai (3 August 2010). "Greasing Their Way: Lipid Modifications Determine Protein Association with Membrane Rafts".
762: 344:. The addition of myristoyl-CoA to a protein can occur during protein translation or after. During co-translational addition of the myristoyl group, the 858:
assembly, budding and further maturation. In order to prevent viral infectivity, myristoylation of the matrix protein could become a good drug target.
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Martin, Dale D.O.; Beauchamp, Erwan; Berthiaume, Luc G. (January 2011). "Post-translational myristoylation: Fat matters in cellular life and death".
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HIV-1 utilizes myristoylation on the Matrix protein to target the viral proteins and viral genome to the membrane for budding and viral maturation.
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Wall, Mark A.; Coleman, David E.; Lee, Ethan; Iñiguez-Lluhi, Jorge A.; Posner, Bruce A.; Gilman, Alfred G.; Sprang, Stephen R. (December 1995).
771:. It is phosphorylated and dephosphorylated to turn signaling on and off. Proto-oncogene tyrosine-protein kinase Src must be localized to the 1610:
McLaughlin, Stuart; Aderem, Alan (July 1995). "The myristoyl-electrostatic switch: a modulator of reversible protein–membrane interactions".
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of the membrane and the positive surface of the associating protein. This allows tighter association and directed localization of proteins.
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171. This polarizes the carbonyl so that there is a net positive charge on the carbon, making it susceptible to nucleophilic attack by the
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of NMT reveals two identical subunits, each with its own myristoyl CoA binding site. Each subunit consists of a large saddle-shaped
123:. Myristoylation allows for weak protein–protein and protein–lipid interactions and plays an essential role in membrane targeting, 155:-terminal blocking group was further characterized as myristic acid. Both labs made this discovery utilizing similar techniques: 714: 582:
of the modified protein. Though the myristoyl group is added onto the end of the protein, in some cases it is sequestered within
1738:-myristoylated proteins, key components in intracellular signal transduction systems enabling rapid and flexible cell responses" 627: 174: 124: 494: 203: 368:
cleavage event, resulting in the exposure of an internal glycine residue, which is then available for myristic acid addition.
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Upon ligand binding to a myristoylated protein, the myristoyl group is exposed and available to associate with the membrane.
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of cells. This lipidation event is the most common type of fatty acylation and is present in many organisms, including
705:, or programmed cell death. Apoptosis is necessary for cell homeostasis and occurs when cells are under stress such as 1961: 1252:-terminal blocking group of the catalytic subunit of cyclic AMP-dependent protein kinase from bovine cardiac muscle" 284:
residue of the protein to be modified. When myristoyl CoA binds, NMT reorients to allow binding of the peptide. The
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Bhatnagar, RS; FĂĽtterer, K; Waksman, G; Gordon, JI (Nov 23, 1999). "The structure of myristoyl-CoA:protein
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Mohammadzadeh, Fatemeh; Hosseini, Vahid; Mehdizadeh, Amir; Dani, Christian; Darabi, Masoud (2018-11-30).
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site, thus inhibiting enzymatic activity and eliminating the parasite from the bloodstream of mice with
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is a gene that codes for proto-oncogene tyrosine-protein kinase Src, a protein important for normal
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Facilitates the association of FSP1 with the lipid-bilayer which enables ferroptosis resistance.
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residue. Myristic acid is a 14-carbon saturated fatty acid (14:0) with the systematic name of
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Aitken, A; Cohen, P; Santikarn, S; Williams, DH; Calder, AG; Smith, A; Klee, CB (Dec 27, 1982).
870:. Myristoylation has been shown to be necessary for the survival of a number of disease-causing 685:
in plant responses to environmental stress. In addition, in signal transduction via G protein,
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can facilitate more tightly regulated protein localization, specifically targeting proteins to
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in order to phosphorylate other downstream targets; myristoylation is responsible for this
2723: 2423: 2314: 2190: 2149: 1083:"A method for the gross analysis of global protein acylation by gas-liquid chromatography" 851: 772: 666: 323: 55: 24: 1919:
Hearps, AC; Jans, DA (Mar 2007). "Regulating the functions of the HIV-1 matrix protein".
721:. Caspase 3 cleaves a number of proteins that are subsequently myristoylated by NMT. The 1753: 1549: 1267: 2585: 2479: 2456: 2398: 2248: 2230: 2117: 1770: 1733: 1674: 1649: 1648:
Wright, Megan H.; Heal, William P.; Mann, David J.; Tate, Edward W. (7 November 2009).
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Kara, UA; Stenzel, DJ; Ingram, LT; Bushell, GR; Lopez, JA; Kidson, C (Apr 1988).
182:-myristoyltransferase with bound myristoyl-CoA. Myristoyl-CoA (red). PDB ID: 3IU1 84:-tetradecanoic acid. This modification can be added either co-translationally or 2525: 2484: 2413: 2378: 2373: 2332: 2304: 2271: 2253: 2225: 2078: 2068: 2058: 2030: 973: 941: 895: 866:
Certain NMTs are therapeutic targets for development of drugs against bacterial
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at membranes or allowing dissociation of myristoylated proteins from membranes.
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Post-translational myristoylation up-regulates apoptotic properties and induces
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Proceedings of the National Academy of Sciences of the United States of America
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to a myristoylated protein with its myristoyl group sequestered can cause a
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Post-translational myristoylation after caspase cleavage targets protein to
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of that protein to the cytoplasm following dissociation from the membrane.
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Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids
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Post-translational myristoylation up-regulates anti-apoptotic properties
2782: 2778: 2774: 2711: 2684: 2626: 2577: 2573: 2471: 2418: 2240: 2182: 2164: 938: 899: 738: 456: 341: 313: 269: 238:. The symmetry of the fold is pseudo twofold. Myristoyl CoA binds at the 151:-tetradecanoyl. Almost simultaneously in Claude B. Klee's lab, this same 63: 1761: 2742: 2734: 2715: 2688: 2499: 1966: 934: 365: 349: 281: 277: 77: 1710: 745:
are three other proteins that are myristoylated following cleavage by
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in the enzyme that allows the release of the myristoylated peptide.
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is responsible for the irreversible addition of a myristoyl group to
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Carr, SA; Biemann, K; Shoji, S; Parmelee, DC; Titani, K (Oct 1982).
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Co-translational myristoylation aids in plasma membrane association
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Co-translational myristoylation aids in plasma membrane association
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is one such protein that once myristoylated, translocates to the
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pathways and is referred to as the dual fatty acylation switch.
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is stabilized by the interaction between a positively charged
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Myristoyl-conformational switches can come in several forms.
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Myristoylation plays a vital role in membrane targeting and
1832: 1830: 1318:-terminal blocking group of calcineurin B as myristic acid" 432:
actin cross-linking when phosphorylated by protein kinase C
1534:"FSP1 is a glutathione-independent ferroptosis suppressor" 2724:
4-(p-hydroxybenzylidene)-5-imidazolinone (HBI) formation
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pro-apoptotic BH3-interacting domain death agonist (Bid)
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is positioned in its binding pocket of NMT so that the
1795:"The structure of the G protein heterotrimer Giα1β1γ2" 503:-terminus myristoylation aids in membrane association 143:-terminal blocking group" on the catalytic subunit of 1643: 1641: 1605: 1603: 1601: 1463:"Overview of Post-Translational Modifications (PTMs)" 526:
Apoptosis-inducing factor mitochondria-associated 2 (
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Hanahan, Douglas; Weinberg, Robert A. (March 2011).
1051: 1049: 1005: 1003: 406:Post-translational myristoylation during apoptosis 2773: 2763: 2733: 2706: 2679: 2669: 2643: 2621: 2599: 2572: 2562: 2540: 2516: 2498: 2470: 2364: 2346: 2323: 2285: 2262: 2239: 2181: 2136: 2126: 2093: 2049: 2013: 1478:"Regulation of G proteins by covalent modification" 260:The addition of the myristoyl group proceeds via a 2697:p-Hydroxybenzylidene-imidazolinone (HBI) formation 1056:Tamanoi, Fuyuhiko; Sigman, David S., eds. (2001). 1011: 1962:PlantsP: Plant-Specific Myristoylation Predictor 336:Co-translational vs. post-translational addition 288:-terminus of NMT then acts as a general base to 890:bacteria, the NMTs of numerous disease-causing 1650:"Protein myristoylation in health and disease" 1476:Chen, Katherine A.; Manning, David R. (2001). 39:Co-translational addition of myristic acid by 1987: 1237: 1235: 8: 2657:Tryptophan tryptophylquinone (TTQ) formation 1516:: CS1 maint: multiple names: authors list ( 1038:: CS1 maint: multiple names: authors list ( 634:Dual modifications of myristoylated proteins 316:anion. Free CoA is then released, causing a 947:has been identified that selectively binds 789:transforming normal cells into cancer cells 497:trafficking and actin remodeling regulation 139:In 1982, Koiti Titani's lab identified an " 2770: 2676: 2569: 2133: 1994: 1980: 1972: 1880:"Hallmarks of Cancer: The Next Generation" 1742:Proceedings of the Japan Academy, Series B 477:cell growth, mobility, survival stimulator 262:nucleophilic addition-elimination reaction 1895: 1854: 1810: 1769: 1732:HAYASHI, Nobuhiro; TITANI, Koiti (2010). 1673: 1565: 1493: 1333: 1285: 1275: 1215: 1155: 1098: 1010:Cox, David L. Nelson, Michael M. (2005). 1018:(4th ed.). New York: W.H. Freeman. 598:to occur between the negatively charged 380: 214:, both of which are members of the GCN5 2751:Methylidene-imidazolone (MIO) formation 1196:"The Biology and Enzymology of Protein 999: 898:as well. Proper NMT functioning in the 47:-terminal glycine of a nascent protein. 1509: 1307: 1305: 1031: 701:Myristoylation is an integral part of 360:residue in the newly forming, growing 352:is modified following cleavage of the 2635:Lysine tyrosylquinone (LTQ) formation 862:Prokaryotic and eukaryotic infections 327:Myristoylation addition mechanism by 127:and functions widely in a variety of 54:is a lipidation modification where a 7: 1921:AIDS Research and Human Retroviruses 1014:Lehninger principles of biochemistry 665:Myristoylation is often followed by 2108:Glycosyl phosphatidylinositol (GPI) 779:event. Increased myristoylation of 658:dual modification is important for 623:guanine nucleotide exchange factors 145:cyclic AMP-dependent protein kinase 894:organisms have been identified as 178:Crystal structure of human type-I 14: 2419:Oxidative deamination to aldehyde 1837:Shoji, S; Kubota, Y (Feb 1989). 1194:Farazi, T. A. (29 August 2001). 729:where it prompts the release of 715:death-inducing signaling complex 560: 548: 304:of myristoyl-CoA. The resulting 2820:Post-translational modification 2007:posttranslational modifications 1204:Journal of Biological Chemistry 540:Myristoylation molecular switch 518:Contains a Ca/myristoyl switch 461:Actin filament-severing protein 272:faces two amino acid residues, 190:-myristoyltransferase (NMT) or 70:to the alpha-amino group of an 1612:Trends in Biochemical Sciences 799:", among them upregulation of 1: 1624:10.1016/S0968-0004(00)89042-8 1440:10.1016/s1388-1981(99)00155-9 1148:10.1128/IAI.56.4.903-909.1988 838:-terminal–most domain of the 1856:10.1248/yakushi1947.109.2_71 1812:10.1016/0092-8674(95)90220-1 1398:10.1016/j.biochi.2010.10.018 1335:10.1016/0014-5793(82)80759-x 628:protein–protein interactions 125:protein–protein interactions 2226:Topaquinone (TPQ) formation 1654:Journal of Chemical Biology 795:can lead to the so-called " 741:and p21-activated kinase 2 416:Apoptosis promoting protein 312:and the negatively charged 93:-myristoyltransferase (NMT) 31:, pictured above) is added. 2841: 1967:ExPASy Myristoylation Tool 1897:10.1016/j.cell.2011.02.013 660:G protein-coupled receptor 596:electrostatic interactions 2670:Crosslinks between three 2003:Protein primary structure 1666:10.1007/s12154-009-0032-8 1558:10.1038/s41586-019-1707-0 1314:"Identification of the NH 989:Glycophosphatidylinositol 957:African sleeping sickness 925:African sleeping sickness 638:Further modifications on 196:-tetradecanoyltransferase 99:addition reaction in the 43:-myristoyltransferase to 2764:Crosslinks between four 1426:-myristoyltransferase". 1248:-Tetradecanoyl is the NH 733:leading to cell death. 390:Myristoylation Function 306:tetrahedral intermediate 2563:Crosslinks between two 1277:10.1073/pnas.79.20.6128 787:and be responsible for 514:Neuronal calcium sensor 475:Serine/threonine kinase 252:end binds the protein. 16:Lipidation modification 2211:Porphyrin ring linkage 1495:10.1038/sj.onc.1204185 1217:10.1074/jbc.R100042200 1136:Infection and Immunity 820: 753:Impact on human health 421:mitochondrial membrane 377:Myristoylated proteins 332: 331:-myristoyltransferase. 183: 48: 32: 2272:Succinimide formation 1933:10.1089/aid.2006.0108 818: 803:, proliferation, and 783:can lead to enhanced 611:conformational change 580:cellular localization 326: 318:conformational change 177: 170:-myristoyltransferase 38: 23:In myristoylation, a 22: 2026:Protein biosynthesis 1465:. Thermo Scientific. 951:, competing for the 832:Viral matrix protein 576:membrane association 204:post-translationally 86:post-translationally 2825:Signal transduction 1762:10.2183/pjab.86.494 1754:2010PJAB...86..494H 1550:2019Natur.575..693D 1268:1982PNAS...79.6128C 1210:(43): 39501–39504. 910:Leishmania donovani 797:hallmarks of cancer 683:signal transduction 677:Signal transduction 653:Myristoylation and 264:. First, myristoyl 245:portion, while the 129:signal transduction 2356:Transglutamination 1058:Protein lipidation 920:Trypanosoma brucei 821: 785:cell proliferation 777:membrane targeting 689:of the α subunit, 600:phospholipid heads 403:structural protein 387:Physiological Role 333: 184: 161:gas chromatography 49: 33: 2807: 2806: 2803: 2802: 2759: 2758: 2665: 2664: 2558: 2557: 2310:Polyglutamylation 2196:Dephosphorylation 2155:Dephosphorylation 1957:The MYR Predictor 1711:10.1021/bi100882y 1705:(30): 6305–6316. 1544:(7784): 693–698. 1488:(13): 1643–1652. 1067:978-0-12-122722-7 984:Palmitoleoylation 886:. In addition to 811:Viral infectivity 537: 536: 300:to attack at the 296:, activating the 228:crystal structure 216:acetyltransferase 157:mass spectrometry 2832: 2771: 2677: 2613:Sulfilimine bond 2591:ADP-ribosylation 2570: 2490:ADP-ribosylation 2409:ADP-ribosylation 2300:ADP-ribosylation 2277:ADP-ribosylation 2201:ADP-ribosylation 2173:ADP-ribosylation 2134: 2127:Single specific 1996: 1989: 1982: 1973: 1945: 1944: 1916: 1910: 1909: 1899: 1875: 1869: 1868: 1858: 1834: 1825: 1824: 1814: 1805:(6): 1047–1058. 1790: 1784: 1783: 1773: 1729: 1723: 1722: 1694: 1688: 1687: 1677: 1645: 1636: 1635: 1607: 1596: 1595: 1569: 1528: 1522: 1521: 1515: 1507: 1497: 1473: 1467: 1466: 1458: 1452: 1451: 1419: 1410: 1409: 1381: 1356: 1355: 1337: 1309: 1300: 1299: 1289: 1279: 1239: 1230: 1229: 1219: 1200:-Myristoylation" 1191: 1170: 1169: 1159: 1127: 1121: 1120: 1102: 1100:10.1002/iub.1975 1078: 1072: 1071: 1053: 1044: 1043: 1037: 1029: 1017: 1007: 904:Leishmania major 846:can assemble at 791:. Activation of 589:molecular switch 564: 552: 381: 266:coenzyme A (CoA) 2840: 2839: 2835: 2834: 2833: 2831: 2830: 2829: 2810: 2809: 2808: 2799: 2755: 2729: 2702: 2661: 2639: 2617: 2595: 2554: 2550:C-mannosylation 2536: 2512: 2494: 2466: 2432:Imine formation 2360: 2342: 2319: 2315:Polyglycylation 2281: 2258: 2235: 2191:Phosphorylation 2177: 2150:Phosphorylation 2122: 2089: 2045: 2009: 2000: 1953: 1948: 1918: 1917: 1913: 1877: 1876: 1872: 1843:Yakugaku Zasshi 1836: 1835: 1828: 1792: 1791: 1787: 1731: 1730: 1726: 1696: 1695: 1691: 1647: 1646: 1639: 1609: 1608: 1599: 1530: 1529: 1525: 1508: 1475: 1474: 1470: 1461:Snider, Jared. 1460: 1459: 1455: 1434:(2–3): 162–72. 1421: 1420: 1413: 1383: 1382: 1359: 1317: 1311: 1310: 1303: 1262:(20): 6128–31. 1251: 1241: 1240: 1233: 1193: 1192: 1173: 1129: 1128: 1124: 1080: 1079: 1075: 1068: 1055: 1054: 1047: 1030: 1026: 1009: 1008: 1001: 997: 965: 953:peptide binding 864: 852:plasma membrane 840:gag polyprotein 813: 773:plasma membrane 769:mitotic cycling 760: 755: 699: 679: 667:phosphorylation 636: 572: 571: 570: 569: 568: 565: 557: 556: 553: 542: 482:plasma membrane 379: 374: 338: 295: 258: 224: 172: 137: 66:attached by an 58:, derived from 56:myristoyl group 25:myristoyl group 17: 12: 11: 5: 2838: 2836: 2828: 2827: 2822: 2812: 2811: 2805: 2804: 2801: 2800: 2798: 2797: 2791: 2789: 2768: 2761: 2760: 2757: 2756: 2754: 2753: 2747: 2745: 2731: 2730: 2728: 2727: 2720: 2718: 2704: 2703: 2701: 2700: 2693: 2691: 2674: 2667: 2666: 2663: 2662: 2660: 2659: 2653: 2651: 2641: 2640: 2638: 2637: 2631: 2629: 2619: 2618: 2616: 2615: 2609: 2607: 2597: 2596: 2594: 2593: 2588: 2586:Disulfide bond 2582: 2580: 2567: 2560: 2559: 2556: 2555: 2553: 2552: 2546: 2544: 2538: 2537: 2535: 2534: 2529: 2522: 2520: 2514: 2513: 2511: 2510: 2504: 2502: 2496: 2495: 2493: 2492: 2487: 2482: 2480:Citrullination 2476: 2474: 2468: 2467: 2465: 2464: 2459: 2457:Propionylation 2454: 2449: 2444: 2439: 2434: 2429: 2427:-glycosylation 2421: 2416: 2411: 2406: 2401: 2399:Ubiquitination 2396: 2391: 2386: 2381: 2376: 2370: 2368: 2362: 2361: 2359: 2358: 2352: 2350: 2344: 2343: 2341: 2340: 2335: 2329: 2327: 2321: 2320: 2318: 2317: 2312: 2307: 2302: 2297: 2291: 2289: 2283: 2282: 2280: 2279: 2274: 2268: 2266: 2260: 2259: 2257: 2256: 2251: 2249:Palmitoylation 2245: 2243: 2237: 2236: 2234: 2233: 2231:Detyrosination 2228: 2223: 2221:Flavin linkage 2218: 2213: 2208: 2203: 2198: 2193: 2187: 2185: 2179: 2178: 2176: 2175: 2170: 2162: 2157: 2152: 2146: 2144: 2131: 2124: 2123: 2121: 2120: 2118:Detyrosination 2115: 2110: 2105: 2099: 2097: 2091: 2090: 2088: 2087: 2084:Myristoylation 2081: 2076: 2071: 2066: 2061: 2055: 2053: 2047: 2046: 2044: 2043: 2041:N–O acyl shift 2038: 2033: 2028: 2023: 2017: 2015: 2011: 2010: 2001: 1999: 1998: 1991: 1984: 1976: 1970: 1969: 1964: 1959: 1952: 1951:External links 1949: 1947: 1946: 1911: 1890:(5): 646–674. 1870: 1826: 1785: 1748:(5): 494–508. 1724: 1689: 1637: 1618:(7): 272–276. 1597: 1523: 1468: 1453: 1411: 1357: 1315: 1301: 1249: 1231: 1171: 1122: 1093:(3): 340–346. 1073: 1066: 1045: 1025:978-0716743392 1024: 998: 996: 993: 992: 991: 986: 981: 979:Palmitoylation 976: 971: 964: 961: 863: 860: 812: 809: 759: 756: 754: 751: 698: 695: 687:palmitoylation 678: 675: 655:palmitoylation 635: 632: 607:Ligand binding 566: 559: 558: 554: 547: 546: 545: 544: 543: 541: 538: 535: 534: 531: 524: 520: 519: 516: 511: 505: 504: 498: 492: 486: 485: 478: 472: 466: 465: 462: 459: 453: 452: 449: 443: 437: 436: 433: 430: 424: 423: 417: 414: 408: 407: 404: 398: 392: 391: 388: 385: 378: 375: 373: 370: 337: 334: 302:carbonyl group 293: 257: 254: 234:surrounded by 223: 220: 192:glycylpeptide 171: 165: 136: 133: 95:catalyzes the 52:Myristoylation 27:(derived from 15: 13: 10: 9: 6: 4: 3: 2: 2837: 2826: 2823: 2821: 2818: 2817: 2815: 2796: 2793: 2792: 2790: 2788: 2784: 2780: 2776: 2772: 2769: 2767: 2762: 2752: 2749: 2748: 2746: 2744: 2740: 2736: 2732: 2726:(chromophore) 2725: 2722: 2721: 2719: 2717: 2713: 2709: 2705: 2699:(chromophore) 2698: 2695: 2694: 2692: 2690: 2686: 2682: 2678: 2675: 2673: 2668: 2658: 2655: 2654: 2652: 2650: 2646: 2642: 2636: 2633: 2632: 2630: 2628: 2624: 2620: 2614: 2611: 2610: 2608: 2606: 2605:Hydroxylysine 2602: 2598: 2592: 2589: 2587: 2584: 2583: 2581: 2579: 2575: 2571: 2568: 2566: 2561: 2551: 2548: 2547: 2545: 2543: 2539: 2533: 2532:Adenylylation 2530: 2527: 2524: 2523: 2521: 2519: 2515: 2509: 2508:Hydroxylation 2506: 2505: 2503: 2501: 2497: 2491: 2488: 2486: 2483: 2481: 2478: 2477: 2475: 2473: 2469: 2463: 2460: 2458: 2455: 2453: 2450: 2448: 2447:Succinylation 2445: 2443: 2442:Carbamylation 2440: 2438: 2435: 2433: 2430: 2428: 2426: 2422: 2420: 2417: 2415: 2412: 2410: 2407: 2405: 2402: 2400: 2397: 2395: 2394:Hydroxylation 2392: 2390: 2389:Adenylylation 2387: 2385: 2382: 2380: 2377: 2375: 2372: 2371: 2369: 2367: 2363: 2357: 2354: 2353: 2351: 2349: 2345: 2339: 2338:Glycosylation 2336: 2334: 2331: 2330: 2328: 2326: 2322: 2316: 2313: 2311: 2308: 2306: 2303: 2301: 2298: 2296: 2295:Carboxylation 2293: 2292: 2290: 2288: 2284: 2278: 2275: 2273: 2270: 2269: 2267: 2265: 2261: 2255: 2252: 2250: 2247: 2246: 2244: 2242: 2238: 2232: 2229: 2227: 2224: 2222: 2219: 2217: 2216:Adenylylation 2214: 2212: 2209: 2207: 2204: 2202: 2199: 2197: 2194: 2192: 2189: 2188: 2186: 2184: 2180: 2174: 2171: 2169: 2167: 2163: 2161: 2160:Glycosylation 2158: 2156: 2153: 2151: 2148: 2147: 2145: 2143: 2139: 2135: 2132: 2130: 2125: 2119: 2116: 2114: 2113:O-methylation 2111: 2109: 2106: 2104: 2101: 2100: 2098: 2096: 2092: 2085: 2082: 2080: 2077: 2075: 2072: 2070: 2067: 2065: 2064:Carbamylation 2062: 2060: 2057: 2056: 2054: 2052: 2048: 2042: 2039: 2037: 2034: 2032: 2029: 2027: 2024: 2022: 2019: 2018: 2016: 2012: 2008: 2004: 1997: 1992: 1990: 1985: 1983: 1978: 1977: 1974: 1968: 1965: 1963: 1960: 1958: 1955: 1954: 1950: 1942: 1938: 1934: 1930: 1926: 1922: 1915: 1912: 1907: 1903: 1898: 1893: 1889: 1885: 1881: 1874: 1871: 1866: 1862: 1857: 1852: 1848: 1844: 1840: 1833: 1831: 1827: 1822: 1818: 1813: 1808: 1804: 1800: 1796: 1789: 1786: 1781: 1777: 1772: 1767: 1763: 1759: 1755: 1751: 1747: 1743: 1739: 1737: 1728: 1725: 1720: 1716: 1712: 1708: 1704: 1700: 1693: 1690: 1685: 1681: 1676: 1671: 1667: 1663: 1659: 1655: 1651: 1644: 1642: 1638: 1633: 1629: 1625: 1621: 1617: 1613: 1606: 1604: 1602: 1598: 1593: 1589: 1585: 1581: 1577: 1573: 1568: 1567:10044/1/75345 1563: 1559: 1555: 1551: 1547: 1543: 1539: 1535: 1527: 1524: 1519: 1513: 1505: 1501: 1496: 1491: 1487: 1483: 1479: 1472: 1469: 1464: 1457: 1454: 1449: 1445: 1441: 1437: 1433: 1429: 1425: 1418: 1416: 1412: 1407: 1403: 1399: 1395: 1391: 1387: 1380: 1378: 1376: 1374: 1372: 1370: 1368: 1366: 1364: 1362: 1358: 1353: 1349: 1345: 1341: 1336: 1331: 1327: 1323: 1319: 1308: 1306: 1302: 1297: 1293: 1288: 1283: 1278: 1273: 1269: 1265: 1261: 1257: 1253: 1247: 1238: 1236: 1232: 1227: 1223: 1218: 1213: 1209: 1205: 1201: 1199: 1190: 1188: 1186: 1184: 1182: 1180: 1178: 1176: 1172: 1167: 1163: 1158: 1153: 1149: 1145: 1141: 1137: 1133: 1126: 1123: 1118: 1114: 1110: 1106: 1101: 1096: 1092: 1088: 1084: 1077: 1074: 1069: 1063: 1059: 1052: 1050: 1046: 1041: 1035: 1027: 1021: 1016: 1015: 1006: 1004: 1000: 994: 990: 987: 985: 982: 980: 977: 975: 972: 970: 967: 966: 962: 960: 958: 954: 950: 946: 943: 940: 936: 932: 931: 930:P. falciparum 926: 922: 921: 916: 915:leishmaniasis 912: 911: 906: 905: 901: 897: 893: 889: 885: 884: 883:C. neoformans 879: 878: 874:, among them 873: 869: 861: 859: 857: 853: 849: 845: 841: 837: 833: 829: 825: 817: 810: 808: 806: 802: 798: 794: 790: 786: 782: 778: 774: 770: 766: 765: 757: 752: 750: 748: 744: 740: 736: 732: 728: 724: 720: 716: 712: 708: 704: 696: 694: 692: 688: 684: 676: 674: 672: 671:translocation 668: 663: 661: 656: 651: 649: 645: 641: 633: 631: 629: 624: 620: 616: 612: 608: 603: 601: 597: 592: 590: 585: 581: 577: 563: 551: 539: 532: 529: 525: 522: 521: 517: 515: 512: 510: 507: 506: 502: 499: 496: 493: 491: 488: 487: 484:localization 483: 479: 476: 473: 471: 468: 467: 463: 460: 458: 455: 454: 450: 448: 444: 442: 439: 438: 434: 431: 429: 426: 425: 422: 418: 415: 413: 410: 409: 405: 402: 399: 397: 394: 393: 389: 386: 383: 382: 376: 371: 369: 367: 363: 359: 355: 351: 347: 343: 335: 330: 325: 321: 319: 315: 311: 310:oxyanion hole 307: 303: 299: 291: 287: 283: 279: 275: 274:phenylalanine 271: 267: 263: 255: 253: 251: 249: 244: 242: 237: 233: 229: 221: 219: 218:superfamily. 217: 213: 209: 205: 201: 197: 195: 189: 181: 176: 169: 166: 164: 162: 158: 154: 150: 146: 142: 134: 132: 130: 126: 122: 118: 114: 110: 106: 102: 98: 97:myristic acid 94: 92: 87: 83: 79: 76: 74: 69: 65: 61: 60:myristic acid 57: 53: 46: 42: 37: 30: 29:myristic acid 26: 21: 2462:Butyrylation 2424: 2165: 2083: 2036:Racemization 2021:Peptide bond 1927:(3): 341–6. 1924: 1920: 1914: 1887: 1883: 1873: 1849:(2): 71–85. 1846: 1842: 1802: 1798: 1788: 1745: 1741: 1735: 1727: 1702: 1699:Biochemistry 1698: 1692: 1660:(1): 19–35. 1657: 1653: 1615: 1611: 1541: 1537: 1526: 1512:cite journal 1485: 1481: 1471: 1456: 1431: 1427: 1423: 1392:(1): 18–31. 1389: 1385: 1328:(2): 314–8. 1325: 1322:FEBS Letters 1321: 1259: 1255: 1245: 1207: 1203: 1197: 1142:(4): 903–9. 1139: 1135: 1125: 1090: 1086: 1076: 1057: 1013: 948: 928: 918: 908: 902: 896:drug targets 881: 875: 865: 835: 822: 801:angiogenesis 792: 780: 763: 761: 731:cytochrome c 727:mitochondria 700: 680: 664: 652: 639: 637: 604: 593: 573: 527: 500: 401:Cytoskeleton 353: 345: 339: 328: 285: 259: 247: 240: 225: 199: 193: 187: 185: 179: 167: 152: 148: 140: 138: 90: 81: 72: 51: 50: 44: 40: 2526:Diphthamide 2485:Methylation 2452:Lactylation 2414:Deamination 2404:Sumoylation 2379:Acetylation 2374:Methylation 2333:Deamidation 2305:Methylation 2254:Prenylation 2079:Methylation 2069:Formylation 2059:Acetylation 2031:Proteolysis 974:Prenylation 942:sulfonamide 888:prokaryotic 877:C. albicans 848:lipid rafts 691:prenylation 648:lipid rafts 584:hydrophobic 509:Hippocalcin 362:polypeptide 298:amino group 290:deprotonate 186:The enzyme 147:in cows as 2814:Categories 2649:Tryptophan 2645:Tryptophan 2601:Methionine 2542:Tryptophan 2325:Asparagine 2095:C terminus 2051:N terminus 1087:IUBMB Life 995:References 892:eukaryotic 868:infections 828:retrovirus 711:DNA damage 445:Signaling 358:methionine 356:-terminal 348:-terminal 131:pathways. 117:protozoans 68:amide bond 64:covalently 2795:Desmosine 2708:Histidine 2528:formation 2518:Histidine 2437:Glycation 2384:Acylation 2348:Glutamine 2287:Glutamate 2264:Aspartate 2206:Sulfation 2142:Threonine 2103:Amidation 2074:Glycation 1592:204833583 1576:1476-4687 1386:Biochimie 1109:1521-6543 1034:cite book 969:Acylation 949:T. brucei 945:inhibitor 747:caspase 3 719:caspase 3 703:apoptosis 697:Apoptosis 644:acylation 495:vesicular 441:G-Protein 372:Functions 256:Mechanism 250:-terminal 243:-terminal 236:α-helices 222:Structure 135:Discovery 101:cytoplasm 75:-terminal 2783:Allysine 2779:Allysine 2775:Allysine 2712:Tyrosine 2685:Tyrosine 2627:Tyrosine 2578:Cysteine 2574:Cysteine 2472:Arginine 2241:Cysteine 2183:Tyrosine 1941:17411366 1906:21376230 1780:20467215 1719:20583817 1684:19898886 1584:31634899 1504:11313912 1482:Oncogene 1448:10570244 1406:21056615 1352:40889752 1226:11527981 1117:30501005 963:See also 939:pyrazole 900:protozoa 805:invasion 739:gelsolin 457:Gelsolin 342:proteome 314:alkoxide 276:170 and 270:carbonyl 2743:Glycine 2735:Alanine 2716:Glycine 2689:Glycine 2500:Proline 2168:-GlcNAc 2014:General 1865:2545855 1821:8521505 1771:3108300 1750:Bibcode 1675:2816741 1632:7667880 1546:Bibcode 1344:7160476 1296:6959104 1264:Bibcode 1166:3278984 935:malaria 927:), and 850:at the 707:hypoxia 384:Protein 366:caspase 350:glycine 282:glycine 278:leucine 232:β-sheet 121:viruses 105:animals 78:glycine 2787:Lysine 2739:Serine 2681:Serine 2623:Lysine 2366:Lysine 2138:Serine 1939:  1904:  1863:  1819:  1778:  1768:  1717:  1682:  1672:  1630:  1590:  1582:  1574:  1538:Nature 1502:  1446:  1404:  1350:  1342:  1294:  1287:347072 1284:  1224:  1164:  1157:259388 1154:  1115:  1107:  1064:  1022:  834:, the 758:Cancer 447:GTPase 428:MARCKS 292:the NH 109:plants 2086:(Gly) 1588:S2CID 1348:S2CID 872:fungi 856:viral 826:is a 824:HIV-1 793:c-Src 781:c-Src 764:c-Src 735:Actin 528:AIFM2 523:FSP1 396:Actin 113:fungi 62:, is 2005:and 1937:PMID 1902:PMID 1884:Cell 1861:PMID 1817:PMID 1799:Cell 1776:PMID 1715:PMID 1680:PMID 1628:PMID 1580:PMID 1572:ISSN 1518:link 1500:PMID 1444:PMID 1432:1441 1402:PMID 1340:PMID 1292:PMID 1222:PMID 1162:PMID 1113:PMID 1105:ISSN 1062:ISBN 1040:link 1020:ISBN 907:and 880:and 854:for 743:PAK2 617:for 578:and 470:PAK2 226:The 212:NMT2 210:and 208:NMT1 159:and 119:and 2766:AAs 2672:AAs 2565:AAs 2129:AAs 1929:doi 1892:doi 1888:144 1851:doi 1847:109 1807:doi 1766:PMC 1758:doi 1707:doi 1670:PMC 1662:doi 1620:doi 1562:hdl 1554:doi 1542:575 1490:doi 1436:doi 1394:doi 1330:doi 1326:150 1282:PMC 1272:doi 1212:doi 1208:276 1152:PMC 1144:doi 1095:doi 917:), 844:gag 709:or 621:by 619:GTP 615:GDP 591:." 490:Arf 412:Bid 88:. 2816:: 1935:. 1925:23 1923:. 1900:. 1886:. 1882:. 1859:. 1845:. 1841:. 1829:^ 1815:. 1803:83 1801:. 1797:. 1774:. 1764:. 1756:. 1746:86 1744:. 1740:. 1713:. 1703:49 1701:. 1678:. 1668:. 1656:. 1652:. 1640:^ 1626:. 1616:20 1614:. 1600:^ 1586:. 1578:. 1570:. 1560:. 1552:. 1540:. 1536:. 1514:}} 1510:{{ 1498:. 1486:20 1484:. 1480:. 1442:. 1430:. 1414:^ 1400:. 1390:93 1388:. 1360:^ 1346:. 1338:. 1324:. 1320:. 1304:^ 1290:. 1280:. 1270:. 1260:79 1258:. 1254:. 1234:^ 1220:. 1206:. 1202:. 1174:^ 1160:. 1150:. 1140:56 1138:. 1134:. 1111:. 1103:. 1091:71 1089:. 1085:. 1048:^ 1036:}} 1032:{{ 1002:^ 959:. 807:. 737:, 630:. 530:) 163:. 115:, 111:, 107:, 2785:– 2781:– 2777:– 2741:– 2737:– 2714:– 2710:– 2687:– 2683:– 2647:– 2625:– 2603:– 2576:– 2425:O 2166:O 2140:/ 1995:e 1988:t 1981:v 1943:. 1931:: 1908:. 1894:: 1867:. 1853:: 1823:. 1809:: 1782:. 1760:: 1752:: 1736:N 1734:" 1721:. 1709:: 1686:. 1664:: 1658:3 1634:. 1622:: 1594:. 1564:: 1556:: 1548:: 1520:) 1506:. 1492:: 1450:. 1438:: 1424:N 1408:. 1396:: 1354:. 1332:: 1316:2 1298:. 1274:: 1266:: 1250:2 1246:N 1244:" 1228:. 1214:: 1198:N 1168:. 1146:: 1119:. 1097:: 1070:. 1042:) 1028:. 933:( 923:( 913:( 836:N 640:N 587:" 501:N 354:N 346:N 329:N 294:3 286:C 248:C 241:N 200:N 194:N 188:N 180:N 168:N 153:N 149:n 141:N 91:N 82:n 73:N 45:N 41:N

Index


myristoyl group
myristic acid

myristoyl group
myristic acid
covalently
amide bond
N-terminal
glycine
post-translationally
N-myristoyltransferase (NMT)
myristic acid
cytoplasm
animals
plants
fungi
protozoans
viruses
protein–protein interactions
signal transduction
cyclic AMP-dependent protein kinase
mass spectrometry
gas chromatography

glycylpeptide N-tetradecanoyltransferase
post-translationally
NMT1
NMT2
acetyltransferase

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