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100) prevent the binding of these molecules to CapZ; in turn allowing it to bind to the microfilament. Competition for actin binding sites can also regulate CapZ binding, as seen with filament elongation factors. These factors include ENA/VASP (enabled/vasodilator-stimulated phosphoprotein). CapZ is not regulated by calcium or calmodulin, as seen with other capping proteins, such as
Gelsolin.
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C-terminal made up of an antiparallel β sheet which is composed of five β strands. On one side of the C-terminal, there is a shorter N-terminal helix and a long C-terminal helix. This long C-terminal helix makes up helix 5. The final helix, helix 6 differs in the α and β subunits. The β subunit is longer than the α subunit.
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Experimentation on chicken muscles have indicated that there are certain proteins that inhibit CapZ from binding. This includes PIP2 and other phospholipids. These molecules bind to CapZ itself to prevent it from binding to actin. However, introduction of certain detergents (in this case Triton X
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molecule, made up of an α and β subunit. The α and β subunits are similar in structure. Each subunit is divided into three domains and a shared C-terminal extension. Helix 1-3 is an N-terminal that is composed of three antiparallel helices that are arranged in an up, down, up pattern. Helix 4 is a
85:. This protein helps to stabilize the actin filaments protecting it from assembly and disassembly. The activity regulation of this protein can be done by other regulatory proteins that bind to the actin filaments blocking the CapZ, hence allowing assembly.
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CapZ plays a role in cell movement (cell crawling) by controlling the lengths of the microfilaments. When CapZ is inhibited by regulating factors, microfilament polymerization or depolymerization occurs allowing
319:"Conservation and divergence between cytoplasmic and muscle-specific actin capping proteins: Insights from the crystal structure of cytoplasmic Cap32/34 from Dictyostelium discoideum"
60:
636:
Yang, Feng Hua; Pyle, W. Glen (March 2012). "Reduced cardiac CapZ protein protects hearts against acute ischemia–reperfusion injury and enhances preconditioning".
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to grow out or retract. This polymerization and depolymerization gives the cell the appearance of crawling. When CapZ binds, it halts both of these processes.
368:
Lodish, Harvey; Berk, Arnold; Kaiser, Chris; Krieger, Monty; Bretscher, Antony; Ploegh, Hidde; Amon, Angelika; Scott, Matthew (2012-05-02).
393:
Yang, Fenghua; Aiello, David L.; Pyle, W. Glen (2008-02-01). "Cardiac myofilament regulation by protein phosphatase type 1alpha and CapZ".
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Heiss, Steven; Cooper, John (June 24, 1991). "Regulation of CapZ, an actin capping protein of chicken muscle, by anionic phospholipids".
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Hug, Christopher; Jay, Patrick Y.; Reddy, Indira; McNally, James G.; Bridgman, Paul C.; Elson, Elliot L.; Cooper, John A. (May 1995).
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This image shows the structures of Cap32/34 superposed onto CapZ (in green) over the Cα positions of the entire CP molecules.
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Edwards, Marc; Zwolak, Adam; Schafer, Dorothy A.; Sept, David; Dominguez, Roberto; Cooper, John A. (2014-10-01).
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477:
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Gremm, D.; Wegner, A. (2000-07-01). "Gelsolin as a calcium-regulated actin filament-capping protein".
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A modest reduction in cardiac CapZ protein protects hearts against acute ischemia-reperfusion injury.
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188:"Actin Filament Capping Protein (CapZ): The Story After Crystal Structure Elucidation"
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438:"Capping protein levels influence actin assembly and cell motility in dictyostelium"
270:"Crystal structure of CapZ: structural basis for actin filament barbed end capping"
213:"Crystal structure of CapZ: structural basis for actin filament barbed end capping"
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Yamashita, Atsuko; Maeda, Kayo; Maéda, Yuichiro (1 April 2003).
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CapZ is known to play a role in cell signaling, as it regulates
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CyMoBase - Database of cytoskeletal and motor protein sequences
538:"Capping protein regulators fine-tune actin assembly dynamics"
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Yamashita, Atsuko; Maeda, Kayo; Maéda, Yuichiro (2003-04-01).
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The main function of CapZ is to cap the barbed (plus) end of
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Eckert, C.; Goretzki, A.; Faberova, M.; Kollmar, M. (2012).
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31:, is a capping protein that caps the barbed end of
81:cells. It is located in the Z band of the muscle
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638:Journal of Molecular and Cellular Cardiology
372:(7th ed.). W. H. Freeman. p. 783.
676:at the U.S. National Library of Medicine
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595:European Journal of Biochemistry
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395:Biochemistry and Cell Biology
455:10.1016/0092-8674(95)90080-2
650:10.1016/j.yjmcc.2011.11.013
97:activity in cardiac cells.
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674:CapZ+Actin+Capping+Protein
678:Medical Subject Headings
336:10.1186/1472-6807-12-12
699:Cell adhesion proteins
370:Molecular Cell Biology
323:BMC Structural Biology
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127:Clinical significance
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286:10.1093/emboj/cdg167
229:10.1093/emboj/cdg167
515:10.1021/bi00100a006
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37:muscle cells
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487:2016-11-06
175:References
118:Regulation
47:CapZ is a
615:0014-2956
562:1471-0072
415:1208-6002
237:0261-4189
112:filopodia
83:sarcomere
43:Structure
693:Category
658:22155006
623:10880956
580:25207437
423:18364747
355:22657106
304:12660160
255:12660160
56:Function
571:4271544
523:1653607
464:7758113
346:3472329
680:(MeSH)
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478:"CapZ"
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329:: 12.
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161:CAPZA3
154:CAPZA2
147:CAPZA1
79:muscle
29:CAPPA1
191:(PDF)
168:CAPZB
140:Genes
75:actin
33:actin
654:PMID
619:PMID
611:ISSN
576:PMID
558:ISSN
519:PMID
460:PMID
442:Cell
419:PMID
411:ISSN
374:ISBN
351:PMID
300:PMID
251:PMID
233:ISSN
198:2019
110:and
27:and
25:CAZ1
21:CAPZ
17:CapZ
646:doi
603:doi
599:267
566:PMC
550:doi
511:doi
450:doi
403:doi
341:PMC
331:doi
290:PMC
282:doi
241:PMC
225:doi
95:PKC
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