The platelet cytoskeleton

Platelets

Volumn , Issue , 2007, Pages 75-97

  Hartwig, John H ^a  

^a BRIGHAM AND WOMEN S HOSPITAL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 61849117080     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-012369367-9/50766-7     Document Type: Chapter

References (223)

1. Boyles G., Fox J.E.B., Phillips D.R., Stenberg P.E. Organization of the cytoskeleton in resting, discoid platelets: Preservation of actin filaments by a modified fixation that prevents osmium damage. J Cell Biol 1985, 101:1463-1472.
2. Fox J., Boyles J., Berndt M., Steffen P., Anderson L. Identification of a membrane skeleton in platelets. J Cell Biol 1988, 106:1525-1538.
3. Kenney D., Linck R. The cytoskeleton of unstimulated blood platelets: Structure and composition of the isolated marginal microtubular band. J Cell Sci 1985, 78:1-22.
4. Huxley H. Electron microscopic studies on the structure of natural and synthetic protein filaments from striated muscle. J Mol Biol 1963, 3:281-308.
5. Nachmias V. Cytoskeleton of human platelets at rest and after spreading. J Cell Biol 1980, 86:795-802.
6. Nachmias V.T., Yoshida K.-I. The cytoskeleton of the blood platelet: A dynamic structure. Adv Cell Biol 1988, 2:181-211.
7. Fox J., Aggerbeck L., Berndt M. Structure of the glycoprotein Ib-IX complex from platelet membranes. J Biol Chem 1988, 263:4882-4890.
8. Du X., Harris S., Tetaz T., Ginsberg M., Berndt M. Association of a phospholipase A2 (14-3-3 protein) with the platelet glycoprotein Ib-IX complex. J Biol Chem 1994, 269:18287-18294.
9. Barkalow K., ItalianoJ., Matsuoka Y., Bennett V., Hartwig J. a-Adducin dissociates from F-actin filaments and spectrin during platelet activation. J Cell Biol 2003, 161:557-570.
10. Feng Y., Walsh C. The many faces of filamin: A versatile molecular scaffold for cell motility and signalling. Nature Cell Biol 2004, 6:1034-1038.
11. Takafuta T., Wu G., Murphy G., Shapiro S. Human β-filamin is a new protein that interacts with the cytoplasmic tail of glycoprotein 1bα. J Biol Chem 1998, 273:17531-17533.
12. Thompson T., Chan Y.-M., Hack A., Brosius M., Rajala M., Lidov H., McNally E., Watkins S., Kunkel L. Filamin 2 (FLN2): A muscle-specific sacroglycan interacting protein. J Cell Biol 2000, 148:115-126.
13. Bröcker F., et al. Assignment of human filamin gene FLNB to human chromosome band 3p14.3 and Identification of YACs containing the complete FLNB transcribed regio. Cytogenet Cell Genet 1999, 85:267-268.
14. Barkalow K., Witke W., Kwiatkowski D., Hartwig J. Coordinated regulation of platelet actin filament barbed ends by gelsolin and capping protein. J Cell Biol 1996, 134:389-399.
15. Welch M., Mitchison T. Purifi cation and assay of the platelet Arp2/3 complex. Methods Enzymol 1998, 298:52-61.
16. Falet H., Hoffmeister K., Neujahr R., Hartwig J. Normal Arp2/3 complex activation in Wiskott-Aldrich syndrome platelets. Blood 2002, 100:2113-2122.
17. Falet H., Hoffmeister K., Neujahr R., Italiano J., Stossel T., Southwick F., Hartwig J. Importance of free barbed ends for Arp2/3 complex function in platelets and fi broblasts. Proc Natl Acad Sci USA 2002, 99:16782-16788.
18. Kwiatkowski D.J., Stossel T.P., Orkin S.H., Mole J.E., Colten H.R., Yin H.L. Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain. Nature 1986, 323:455-458.
19. Yin H.L., Stossel T.P. Control of cytoplasmic actin gel-sol transformation by gelsolin, a calciumdependent regulatory protein. Nature 1979, 281:583-586.
20. Janmey P.A., Chaponnier C., Lind S.E., Zaner K.S., Stossel T.P., Yi H.L. Interactions of gelsolin and gelsolin actin complexes with actin. Effects of calcium on actin nucleation, filament severing and end blockin. Biochem 1985, 24:3714-3723.
21. Janmey P.A., Iida K., Yin H.L., Stossel T.P. Polyphosphoinositide micelles and polyphosphoinositidecontaining vesicles dissociate endogenous gelsolin-actin complexes and promote actin assembly from the fast-growing end of actin filaments blocked by gelsolin. J Biol Chem 1987, 262:12228-12236.
22. Kwiatkowski D.J., Janmey P.A., Mole J.E., Yin H.L. Isolation and properties of two actin-binding domains in gelsolin. J Biol Chem 1985, 260:15232-15238.
23. Lind S.E., Janmey P.A., Herbert T., Chaponnier C., Yin H., Stossel T. Interaction of actin with profilin and gelsolin during platelet activation. Blood 1986, 68:321a.
24. Lassing I., Lindberg U. Specificity of the inter action between phosphatidylinositol 4,5-bisphosphate and the profiling: actin complex. J Cell Biochem 1988, 37:255-267.
25. Markey F., Lindberg U., Eriksson L. Human platelets contain profilin, a potential regulator of actin polymerizability. FEBS Lett 1978, 88:75-79.
26. Bamburg J. Proteins of the ADF/Cofilin family: Essential regulators of actin dynamics. Ann Rev Cell Dev 1999, 15:185-230.
27. Ghosh M., Song X., Mouneimne G., Sidani M., Lawrence D., Condeelis J. Cofilin promotes actin polymerization and defines the direction of cell motility. Science 2004, 304:743-746.
28. Yamaguchi H., Lorenz M., Kempiak S., Sarmiento C., Coniglio S., Symons M., Segall J., Eddy R., Miki H., Takenawa T., Condeelis J. Molecular mechanisms of invadopodium formation: The role of the N-WASPArp2/ 3 complex pathway and Cofilin. J Cell Biol 2005, 168:441-452.
29. Nachmias V. Small actin-binding proteins: The β-thymosin family. Curr Opin Cell Biol 1993, 5:56-62.
30. Nachmias V., Cassimeris L., Golla R., Safer D. Thymosin beta 4 (Tβ4) in activated platelets. Eur J Cell Biol 1993, 61:314-320.
31. Safer D., Elzinga M., Nachmias V.T. Thymosin B4 and Fx, an actin-sequestering peptide, are indistinguishable. J Biol Chem 1991, 266:4029-4032.
32. Safer D., Nachmias V. Beta thymosins as actin binding peptides. BioEssays 1994, 16:473-479.
33. Rosenberg S., Stracher A., Burridge K. Isolation and characterization of a calcium-sensitive α-actinin-like protein from human platelet cytoskeletons. J Biol Chem 1981, 256:12986-12991.
34. Adelstein R.S., Conti M.A. Phosphorylation of platelet myosin increases actin activated myosin ATPase activity. Nature 1975, 256:597-598.
35. Takashima T., Matsumura S., Kariya T., Sunaga T., Kumon A. Studies on the physical states of human platelet myosin in crude extracts. J Biochem 1988, 104:1027-1035.
36. Beckerle M., Miller D., Bertagnolli M., Locke S. Activation-dependent redistribution of the adhesion plaque protein, talin, in intact human platelets. J Cell Biol 1989, 109:3333-3346.
37. Knezevic I., Leisner T., Lam S.-T. Direct binding of the platelet integrin αIIbβ3 (GPIIb-IIIa) to talin. J Biol Chem 1996, 271:16416-16421.
38. O'Halloran T., Beckerle M.C., Burridge K. Identification of talin as a major cytoplasmic protein implicated in platelet activation. Nature 1985, 317:449-451.
39. Asyee G.M., Sturk A., Muszbek L. Association of vinculin to the platelet cytoskeleton during thrombininduced aggregation. Exp Cell Res 1987, 168:358-364.
40. Turner C.E., Glenney J.J., Burridge K. Paxillin: A new vinculin-binding protein present in focal adhesions. J Cell Biol 1990, 111(3):1059-1068.
41. Salgia R., Li J.-L., Lo S., Brunkhorst B., Kansas G., Sobhany E., Sun Y., Pisick E., Hallek M., Ernst T., Tantravahi R., Chen L., Griffin J. Molecular cloning of human paxillin, a focal adhesion protein phosphorylated by P210BCR/ABL. J Biol Chem 1995, 270:5039-5047.
42. Crawford A., Michelsen J., Beckerle M. An interaction between zyxin and alpha-actinin. J Cell Biol 1992, 116:1381-1393.
43. Reinhard M., Tripier D., Walter U. Identification, purifi cation and characterization of a zyxin-related protein that binds the focal adhesion and microfilament protein VASP (vasodilator-stimulated phosphoprotein). Proc Natl Acad Sci USA 1995, 92:7956-7960.
44. Reinhard M., Zumbrunn J., Jaquemar D., Kuhn M., Walter U., Trueb B. An α-actinin binding site of zyxin is essential for subcellular zyxin localization and α-actinin recruitment. J Biol Chem 1999, 274:13410-13418.
45. Fischer R., Fritz-Six K., Fowler V. Pointed-end capping by tropomodulin 3 negative regulates endothelial cell motility. J Cell Biol 2003, 161:371-380.
46. Reinhard M., Giehl K., Abel K., Haffner C., Jarchau T., Hoppe V., Jockusch B., Walter U. The prolinerich focal adhesion and microfilament protein VASP is a ligand for profilins. EMBO J 1995, 14:1583-1589.
47. Reinhard M., Rudiger M., Jockusch B., Walter U. VASP interaction with vinculin: A recurring theme of interactions with proline-rich motifs. FEBS Letters 1996, 399:103-107.
48. Reinhard M., Halbrügge M., Scheer U., Wiegand C., Jockusch B.M., Walter U. The 46/50 kDa phosphoprotein VASP purifi ed from human platelets is a novel protein associated with actin filaments and focal contacts. EMBO J 1992, 11:2063-2070.
49. Rottner K., Behrendt B., Small J., Wehland J. VASP dynamics during lamellipodia protrusion. Nature Cell Biol 1999, 5:321-322.
50. Massberg S., Gruner S., Konrad I., Garcia Arguinzonis G., Eigenthaler M., Hemler K., Kersting J., Schulz C., Muller I., Besta F., Niewsandt B., Heinzmann U., Walter U., Gawaz M. Enhanced in vivo platelet adhesion in vasodilator-stimulated phosphoprotein (VASP) -deficient mice. Blood 2004, 103:136-142.
51. Wu H., Parsons J. Cortactin, an 80/85-kilodalton pp60src substrate, is a filamentous actin-binding protein enriched in the cell cortex. J Cell Biol 1993, 120:1417-1426.
52. Weaver A., Heuser J., Karginov A., Lee W., Parsons J., Cooper J. Interaction of cortactin and N-WASp with Arp2/3 complex. Curr Biol 2002, 6:1270-1278.
53. Rohatgi R., Ma L., Miki H., Lopez M., Kirchhausen T., Takenawa T., Kirschner M. The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly. Cell 1999, 97:221-231.
54. Snapper S.B., Rosen F.S. The Wiskott-Aldrich syndrome protein (WASP): Roles in signaling and cytoskeletal organization. Annu Rev Immunol 1999, 17:905-929.
55. Suetsugu S., Miki H., Takenawa T. Identification of two human WAVE/SCAR homologues as general actin regulatory molecules which associate with the Arp2/3 complex. Biochem Biophys Res Commun 1999, 260:296-302.
56. Dahl J., Wang-Dunlop J., Gonzales C., Goad M., Mark R., Kwak S. Characterization of the WAVE1 knock-out mouse: Implications for CNS development. J Neurosci 2003, 23:3343-3352.
57. Oda A., Miki H., Wada I., Yamaguchi H., Yamazaki D., Suetsugu S., Nakajima M., Nakayama A., Okawa K., Miyazaki H., Matsuno K., Ochs H., Machesky L., Fujita H., Takenawa T. WAVE/scars in platelets. Blood 2005, 105:3141-3148.
58. Vaduva G., Martinez-Quiles N., Anton I., Martin N., Geha R., Hopper A., Ramesh N. The human WASP-interacting protein, WIP, activates the cell polarity pathway in yeast. J Biol Chem 1999, 274:17103-17108.
59. Glenney J., Glenney P., Weber K. Erythroid spectrin, brain fodrin, and intestinal brush border proteins (TW-260/240) are related molecules containing a common calmodulin-binding subunit bound to a variant cell type-specific subunit. Proc Natl Acad Sci USA 1982, 79:4002-4005.
60. Shotton D., Burke B., Branton D. The molecular structure of human erythrocyte spectrin. Biophysical and electron microscopic studie. J Mol Biol 1978, 131:303-329.
61. Tyler J., Hargreaves W., Branton D. Purifi cation of two spectrin-binding proteins: Biochemical and electron microscopic evidence for site-specific reassociation between spectrin and bands 2.1 and 4. Proc Natl Acad Sci USA 1979, 76:5192-5196.
62. Tyler J.M., Anderson J.M., Branton D. Structural comparison of several actin-binding molecules. J Cell Biol 1980, 85:489-495.
63. Ungewickell E., Gratzer W. Self-association of human spectrin. A thermodynamic and kinetic stud. Eur J Biochem 1978, 88:379-385.
64. Wasenius V.-M., Saraste M., Salven P., Eramaa M., Holm L., Lehto V.-P. Primary structure of the brain alpha-spectrin. J Cell Biol 1989, 108:79-93.
65. Winkelmann J., Chang J.-G., Tse W., Scarpa A., Marchesi V., Forget B. Full-length sequence of the cDNA for human erythroid β-spectrin. J Biol Chem 1990, 264:11827-11832.
66. Bennett V. Immunoreactive forms of human erythrocyte ankyrin are present in diverse cells and tissues. Nature 1979, 281:597-599.
67. Liu S.-C., Derick L., Palek J. Visualization of the hexogonal lattice in the erythrocyte membrane skeleton. J Cell Biol 1987, 104:527-536.
68. Liu S.-C., Windisch P., Kim S., Palek J. Oligomeric states of spectrin in normal erythrocyte membranes: Biochemical and electron microscopic studies. Cell 1984, 37:587-594.
69. Fowler V., Sussmann M., Miller P., Flucher B., Daniels M. Tropomodulin is associated with the free (pointed) ends of the thin filaments in rat skeletal muscle. J Cell Biol 1993, 120:411-420.
70. Fowler V.M. Tropomodulin: A cytoskeletal protein that binds to the end of erythrocyte tropomyosin and inhibits tropomyosin binding to actin. J Cell Biol 1990, 111:471-482.
71. Nehls V., Drenckhahn D., Joshi R., Bennett V. Adducin in erythrocyte precursor cells of rats and humans: Expression and compartmentalization. Blood 1991, 78:1692-1696.
72. Kuhlman P., Hughes C., Bennett V., Fowler V. A new function for adducin. Calcium/calmodulin-regulated capping of the barbed ends of actin filament. J Biol Chem 1996, 271:7986-7991.
73. Mische S., Mooseker M.S., Morrow J.S. Erythrocyte adducin: A calmodulin-regulated actin-bundling protein that stimulates spectrin-actin binding. J Cell Biol 1987, 105:2837-2845.
74. 2+-dependent protease during platelet activation. Blood 1987, 69:537-545.
75. Hartwig J., DeSisto M. The cytoskeleton of the resting human blood platelet: Structure of the membrane skeleton and its attachment to actin filaments. J Cell Biol 1991, 112:407-425.
76. Hartwig J. Mechanism of actin rearrangements mediating platelet activation. J Cell Biol 1992, 118:1421-1442.
77. Kaiser H., O'Keefe E., Bennett V. Adducin: Ca++-dependent association with sites of cell-cell contact. J Cell Biol 1989, 109:557-569.
78. Matsuoka Y., Li X., Bennett V. Adducin is an in vivo substrate for protein kinase C: Phosphorylation in the MARCKS-related domain inhibits activity in promoting spectrin-actin complexes and occurs in many cells, including dendritic spines of neurons. J Cell Biol 1998, 142:485-497.
79. Matsuoka Y., Li X., Bennett V. Adducin: Structure, function, and regulation. Cell Mot Life Sci 2000, 57:884-895.
80. Wang D., Shaw G. The association of the Cterminal region of betaIepsilon2 spectrin to brain membranes is mediated by a pH domain, does not require membrane proteins, and coincides with an inositol-1,4,5 triphosphate binding site. Biochem Biophys Res Commun 1995, 217:608-615.
81. Rosenberg S., Stracher A. Effect of actin-binding protein on the sedimentation properties of actin. J Cell Biol 1982, 94:51-55.
82. Rosenberg S., Stracher A., Lucas R. Isolation and characterization of actin and actin-binding protein from human platelets. J Cell Biol 1981, 91:201-211.
83. Stossel T., Condeelis J., Cooley L., Hartwig J., Noegel A., Schleicher M., Shapiro S. Filamins as integrators of cell mechanics and signalling. Nature Reviews 2001, 2:138-145.
84. Gorlin J., Yamin R., Egan S., Stewart M., Stossel T., Kwiatkowski D., Hartwig J. Human endothelial actin-binding protein (ABP-280, non-muscle filamin): A molecular leaf spring. J Cell Biol 1990, 111:1089-1105.
85. Fox J. Identification of actin-binding protein as the protein linking the membrane skeleton to glycoproteins on platelet plasma membrane. J Biol Chem 1985, 260:11970-11977.
86. Okita L., Pidard D., Newman P., Montogomery R., Kunicki T. On the association of glycoprotein Ib and actin-binding protein in human platelets. J Cell Biol 1985, 100:317-321.
87. Andrews R., Fox J. Interaction of purifi ed actinbinding protein with the platelet membrane glycoprotein Ib-IX complex. J Biol Chem 1991, 266:7144-7147.
88. Andrews R., Fox J. Identification of a region in the cytoplasmic domain of the platelet membrane glycopro-tein Ib-IX complex that binds to purifi ed actin-binding protein. J Cell Biol 1992, 267:18605-18611.
89. Meyer S., Zuerbig S., Cunninghan C., Hartwig J., Bissel T., Gardner K., Fox J. Identification of the region in actin-binding protein that binds to the cytoplasmic domain of glycoprotein Ibα. J Biol Chem 1997, 272:2914-2919.
90. Fucini P., Al E. Molecular architecture of the rod domain of the dicytostelium gelation factor (ABP-120). J Mol Biol 1999, 291:1017-1023.
91. Ohta Y., Suxuki N., Nakamura S., Hartwig J., Stossel T. The small GTPase RalA targets filamin to induce fi lopodia. Proc Natl Acad Sci USA 1999, 96:2122-2128.
92. Nakamura F., Pudas R., Heikkinen O., Permi P., Kilpeläinen I., Munday A., Hartwig J., Stossel T., Ylänne J. The structure of the GP1b-filamin A complex. Blood 2005, Submitted.
93. Kovacsovics T., Hartwig J. Thrombin-induced GPIb-IX centralization on the platelet surface requires actin assembly and myosin II activation. Blood 1996, 87:618-629.
94. Du X., Fox J., Pei S. Identification of a binding sequence for the 14-3-3 protein within the cytoplasmic domain of the adhesion receptor, platelet glycoprotein Ibα. J Biol Chem 1996, 267:18605.
95. Schwer H., Lecine P., Tiwari S., Italiano J., Hartwi J., Shivdasani R. A lineage-restricted and divergent β tubulin isoform is essential for the biogenesis, structure and function of mammalian blood platelets. Curr Biol 2001, 11:579-586.
96. Italiano J., Bergmeier W., Tiwari S., Falet H., Hartwig J., Fmeister K., Andre P., Wagner D., Shivdasani R. Mechanisms and implications of platelet discoid shape. Blood 2003, 101:4789-4796.
97. White J. Infl uence of taxol on the response of platelets to chilling. Am J Pathol 1982, 108:184.
98. Freson K., De Vos R., Wittevrognel C., Thys C., Defoor J., Vanhees L., Vermylen J., Peerlinck K., Van Geet C. The β1-tubulin Q43P functional polymorphism reduces the risk of cardiovascular disease in men by modulating platelet function and structure. Blood 2005, 106:2356-2362.
99. Rothwell S., Calvert V. Activation of human platelets causes post-translational modifi cations to cytoplasmic dynein. Thromb Haemost 1997, 78:910-918.
100. Gibbons I. The role of dynein in microtubule-based motility. Cell Struct Funct 1996, 21:343-349.
101. Schroer T.A., Steuer E.R., Sheetz M.P. Cytoplasmic dynein is a minus end-directed motor for membranous organelles. Cell 1989, 56(6):937-946.
102. Steuer E.R., Wordeman L., Schroer T.A., Sheetz M.P. Localization of cytoplasmic dynein to mitotic spindles and kinetochores [see comments]. Nature 1990, 345(6272):266-268.
103. Ginsberg M.H., Du X., Plow E. Inside-out integrin signaling. Curr Opin Cell Biol 1992, 4:766-771.
104. Shattil S., Hoxie J., Cunningham M., Brass L. Changes in platelet membrane glycoprotein IIb-IIIa complex during platelet activition. J Biol Chem 1985, 260:11107-11114.
105. Shattil S., Kashiwagi H., Pampori N. Integrin signaling: The platelet paradigm. Blood 1998, 91:2645-2657.
106. Fox J.E.B., Phillips D.R. Inhibition of actin polymerization in blood platelets by cytochalasins. Nature 1981, 292:650-652.
107. Carlier M. Control of actin dynamics. Curr Opin Cell Biol 1998, 10:45-51.
108. Carlier M.-F. Dynamic actin. Curr Biol 1993, 3:321-323.
109. Pollard T.D., Mooseker M.S. Direct measurement of actin polymerization rate constants by electron microscopy of actin filaments nucleated by isolated microvillus cores. J Cell Biol 1981, 88:654-659.
110. Pollard T.D., Weeds A.G. The rate constant for ATP hydrolysis by polymerized actin. FEBS Lett 1984, 170:94-98.
111. Berridge M.J. Inositol trisphosphate and diacylglycerol as second messengers. Biochem 1984, 220:345-360.
112. Sage S., Rink T. The kinetics of changes in intracellular calcium concentration in fura-2-loaded human platelets. J Biol Chem 1987, 262:16364-16369.
113. Brass L. More pieces of the platelet activation puzzle slide into place. J Clin Invest 1999, 104:1663-16654.
114. Vu T., Hung D., Wheaton V., Coughlin S. Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism for receptor activation. Cell 1991, 64:1057-1068.
115. Molino M., Bainton D., Hoxie J., Coughlin S., Brass L. Thrombin receptors on human platelets. J Biol Chem 1997, 272:6011-6017.
116. Kahn M., Nakanishi-Matsui M., Shapiro M., Ishihara H., Coughlin S. Protease-activated receptors 1 and 4 mediate activation of human platelets by thrombin. J Clin Invest 1999, 103:879-887.
117. Shapiro M., Weiss E., Faruqi T., Coughlin S. Protease-activated receptors 1 and 4 are shut off with distinct kinetics after activation by thrombin. J Biol Chem 2000, 275:25216-25221.
118. Watson S.P., Gibbins J. Collagen receptor signalling in platelets: Extending the role of the ITAM. Immunol Today 1998, 19:260-264.
119. McGrath J., Osborn E., Tardy Y., Dewey C., Hartwig J. Regulation of the actin cycle in vivo by actin filament severing. Proc Natl Acad Sci USA 2000, 97:6532-6537.
120. Witke W., Sharpe A., Hartwig J., Azuma T., Stossel T., Kwiatkowski D. Hemostatic, infl ammatory, and fi broblast responses are blunted in mice lacking gelsolin. Cell 1995, 81:41-51.
121. 2+-activated regulatory protein of macrophages. J Biol Chem 1980, 255:9490-9493.
122. Hartwig J., Chambers K., Stossel T. Association of gelsolin with actin filaments and cell membranes of macrophages and platelets. J Cell Biol 1989, 108:467-479.
123. Lind S., Yin H.L., Stossel T.P. Human platelets contain gelsolin, a regulator of actin filament length. J Clin Invest 1982, 69:1384-1387.
124. McLaughlin P., Gooch J., Mannherz H.-G., Weeds A. Structure of gelsolin segment 1-actin complex and the mechanism of filament severing. Nature 1993, 364:685-692.
125. Janmey P., Lamb J., Allen P., Matsudaira P. Phosphoinositide-binding peptides derived from the sequence of gelsolin and villin. J Biol Chem 1992, 267:11818-11823.
126. Janmey P., Stossel T. Modulation of gelsolin function by phosphatidylinositol 4,5-bisphosphate. Nature 1987, 325:362-364.
127. Janmey P., Stossel T. Gelsolin-polyphosphoinositide interaction. Full expression of gelsolin-inhibiting function by polyphosphoinositides in vesicular form and inactivation by dilution, aggregation, or masking of the inositol head group. J Biol Chem 1989, 264:4825-4831.
128. Selve N., Wegner A. Rate of treadmilling of actin filaments in vitro. J Mol Biol 1986, 187:627-631.
129. Selve N., Wegner A. pH-dependent rate of formation of the gelsolin-actin complex from gelsolin and monomeric actin. Eur J Biochem 1987, 168:111-115.
130. Weeds A., Maciver S. F-actin capping proteins. Curr Opin Cell Biol 1993, 5:63-69.
131. Weeds A.G., Harris H., Gratzer W., Gooch J. Interactions of pig plasma gelsolin with G-actin. Eur J Biochem 1986, 161:77-84.
132. 2+-dependent regulatory protein of actin gel sol transformation. Its intracellular distribution in a variety of cells and tissues. J Cell Biol 1981, 91:901-906.
133. Yin H.L., Iida K., Janmey P.A. Identification of a polyphosphoinositide-modulated domain in gelsolin which binds to the sides of actin filaments. J Cell Biol 1988, 106:805-812.
134. 2+ control of actin gelation. J Biol Chem 1980, 255:9494-9500.
135. Meerschaert K., De Corte V., De Ville Y., Vandekerckhove J., Gettemans J. Gelsolin and functionally similar actin-binding proteins are regulated by lysophosphatidic acid. EMBO J 1998, 15:5923-5932.
136. Kurth M., Bryan J. Platelet activation induces the formation of a stable gelsolin-actin complex from monomeric gelsolin. J Biol Chem 1984, 259:7473-7479.
137. Hartwig J., Bokoch G., Carpenter C., Janmey P., Taylor L., Toker A., Stossel T. Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets. Cell 1995, 82:643-653.
138. Carlier M.-F., Didry D., Erk I., Lepault J., Van Troys M., Vanderkerckhove J., Perelroizen I., Yin H., Doi Y., Pantaloni D. Tβ4 is not a simple G-actin sequestering protein and interacts with F-actin at high concentration. J Biol Chem 1996, 271:9231-9239.
139. Carlsson L., Markey F., Blikstad I., Persson T., Lindberg U. Reorganization of actin in platelets stimulated by thrombin as measured by the DNase I inhibition assay. Proc Natl Acad Sci USA 1979, 76:6376-6380.
140. Carlsson L., Nystrom L.E., Sundkvist I., Markey F., Lindberg U. Profilin, a low molecular weight protein controlling actin polymerisability. Contractile systems in non-muscle tissues 1976, Elsevier/North-Holland Biomedical Press, Amsterdam. S.V. Perry, A. Margreth, R.S. Adelstein (Eds.).
141. Carlsson L., Nystrom L.E., Sundkvist I., Markey F., Lindberg U. Actin polymerizability is infl uenced by profilin, a low molecular weight protein in non-muscle cells. J Mol Biol 1977, 115:465-483.
142. Barkalow K., Hartwig J. The role of actin filament barbed-end exposure in cytoskeletal dynamics and cell motility. Biochem Soc Trans 1995, 23:451-456.
143. Lind S.E., Janmey P.A., Chaponnier C., Herbert T.-J., Stossel T.P. Reversible binding of actin to gelsolin and profilin in human platelet extracts. J Cell Biol 1987, 105:833-842.
144. Schafer D., Jennings P., Cooper J. Dynamics of capping protein and actin assembly in vitro: Uncapping barbed ends by polyphosphoinositides. J Cell Biol 1996, 135:169-179.
145. Mejillano M., Kojima S., Applewhite D., Gertler F., Svitkina T., Borisy G. Lamellipodial versus fi lopodial mode of the actin nanomachinery: Pivotal role of the filament barbed end. Cell 2004, 118:363-373.
146. Machesky L., Gould K. The Arp2/3 complex: A multifunctional actin organizer. Curr Opin Cell Biol 1999, 11:117-121.
147. Mullins R., Heuser J., Pollard T. The interaction of Arp2/3 complex with actin: Nucleation, high affi nity pointed end capping, and formation of branched networks of filaments. Proc Natl Acad Sci USA 1998, 95:6181-6186.
148. Machesky L., Atkinson S., Ampe C., Vandekerckhoe J., Pollard T. Purifi cation of a cortical actin complex containing two unconventional actins from Acanthamoeba by affi nity chromatography on profilin-agarose. J Cell Biol 1994, 127:107-115.
149. Welch M., Rosenblatt J., Skoble J., Portnoy D., Mitchison T. Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation. Science 1998, 281:105-108.
150. Laine R., Zeile W., Kang F., Purich D., Southwick F. Vinculin proteolysis unmasks an ActA homolog for actin-based Shigella motility. J Cell Biol 1997, 138:1255-1264.
151. Beckerle M. Spatial control of actin filament assembly: Lessons from. Listeria. Cell 1998, 95:741-748.
152. Bear J., Rawls J., Saxe III C. SCAR, a WASPrelated protein, isolated as a suppressor of receptor defects in late Dictyostelium development. J Cell Biol 1998, 142:1325-1335.
153. Machesky L., Mullins R., Higgs H., Kaiser D., Blanchoin L., May R., Hall M., Pollard T. SCAR, a WASprelated protein, activates dendritic nucleation of actin filaments by the ARP2/3 complex. Proc Natl Acad Sci USA 1999, 96:3739-3744.
154. Miki H., Miura K., Takenawa T. N-WASP, a novel actin-depolymerizing protein, regulates the cortical cytoskeletal rearrangement in a PIP2-dependent manner downstream of tyrosine kinases. EMBO J 1996, 15:5326-5335.
155. Miki H., Sasaki T., Takai Y., Takenawa T. Induction of fi lopodium formation by a WASP-related actindepolymerizing protein N-WASP. Nature 1998, 391:93-96.
156. Miki H., Suetsugu S., Takenawa T. WAVE, a novel WASP-family protein involved in actin reorganization induced by Rac. EMBO J 1998, 17:6932-6941.
157. Winter D., Lechler T., Li R. Activation of the yeast Arp2/3 complex by Bee1p, a WASP-family protein. Curr Biol 1999, 9:501-506.
158. Aspenstrom P., Lindberg U., Hall A. The two GTPases, Cdc42 and Rac, bind directly to a protein implicated in the immunodefi ciency disorder Wiskott-Aldrich syndrome. Curr Biol 1996, 6:70-75.
159. Derry J., Ochs H., Francke U. Identification of a novel gene mutated in Wiskott-Aldrich syndrome. Cell 1994, 78:635-644.
160. Kolluri R., Tolias K., Carpenter C., Rosen F., Kirchhausen T. Direct interaction of the Wiskott-Aldrich syndrome protein with the GTPase, Cdc42. Proc Natl Acad Sci USA 1996, 93:5615-5618.
161. Symons M., Derry J., Karlak B., Jiang S., Lemahieu V., McCormick F., Francke U., Abo A. Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization. Cell 1996, 84:723-734.
162. Snapper S., Rosen F., Mizoguchi E., Cohen P., Khan W., Liu C., Hagemann T., Kwan S., Ferrini R., Davidson L., Bhan A., Alt F. Wiskott-Aldrich syndrome protein-defi cient mice reveal a role for WASP in T but not B cell activation. Immunity 1998, 9:81-91.
163. Snapper S., Takeshima F., Anton I., Liu C.-H., Thomas S., Nguyen D., Dudley D., Fraser H., Purich D., Klein C., Bronson R., Mulligan R., Southwick F., Geha R., Goldberg M., Rosen F., Hartwig J., Alt F. NWASP defi ciency reveals distinct pathways for cell surface projections and the actin-based motility of intracellular microorganisms. Nature Cell Biol 2001, 3:897-904.
164. Ramesh N., Antón I., Martínez-Quiles N., Geha R. Waltzing with WASP. Trends Cell Biol 1999, 9:15-19.
165. Egile C., Loisel T., Laurent V., Li R., Pantaloni D., Sansonetti S., Carlier M.-F. Activation of the CDC42 effector N-WASP by the Shigella fl exneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility. J Cell Biol 1999, 146:1319-1332.
166. Higgs H., Pollard T. Activation by Cdc42 and PIP2 of Wiskott-Aldrich syndrome protein (WASp) stimulates actin nucleation by Arp2/3 complex. J Cell Biol 2000, 150:1311-1320.
167. Uruno T.J., Zhang P., Fan Y.-X., Egile C., Li R., Mueller S., Zhan X. Activation of Arp2/3 complexmediated actin polymerization by cortactin. Nature Cell Biol 2001, 3:259-266.
168. Ozawa K., Kashiwada K., Takahashi M., Sobue K. Translocation of cortactin (p80/85) to the actinbased cytoskeleton during thrombin receptor-mediated platelet activation. Exp Cell Res 1995, 221:197-204.
169. Weed S., Karginov V., Schafer D., Weaver A., Kinley A., Cooper J., Parsons J. Cortactin localization to sites of actin assembly in lamellipodia requires interactions with F-actin and the Arp2/3 complex. J Cell Biol 2000, 151:29-40.
170. Head J., Jiang D., Li M., Zorn L., Schaefer E., Parsons J., Weed S. Cortactin tyrosine phosphorylation requires rac1 activity and association with the cortical actin cytoskeleton. Mol Biol Cell 2003, 14:3216-3229.
171. Goode B., Rodal A., Barnes G., Drubin D. Activation of the Arp2/3 complex by the actin filament binding protein Abp1p. J Cell Biol 2001, 153:627-634.
172. Janmey P. Phosphoinositides and calcium as regulators of cellular actin assembly and disassembly. Annu Rev Physiol 1994, 56:169-191.
173. Janmey P. The cytoskeleton and cell signaling component localization and mechanical coupling. Physiol Rev 1998, 78:763-781.
174. Kovacsovics T., Bachelot C., Toker A., Vlahos C., Duckworth B., Cantley L., Hartwig J. Phosphoinositide 3-kinase inhibition spares actin assembly in activating platelets, but reverses platelet aggregation. J Biol Chem 1995, 270:11358-11366.
175. Tolias K., Hartwig J., Ishihara H., Shibisaki Y., Erickson J., Cantley L., Carpenter C. Type Iα phosphatidylinositol-4-phosphate 5-kinase mediates Rac-dependent actin assembly. Curr Biol 2000, 10:153-156.
176. Abrams C., Zhang J., Downes C., Tang X., Zhao W., Rittenhouse S. Phosphopleckstrin inhibits Gβγ-activable platelet phosphatidylinositol-4,5-bisphosphate 3-kinase. J Biol Chem 1996, 271:25192-25197.
177. Tolias K., Cantley L., Carpenter C. Rho family GTPases bind to phosphoinositide kinases. J Biol Chem 1995, 270:17656-17659.
178. Honda A., Nogami M., Yokozeki T., Yamazaki M., Nakamura H., Watanage H., Kawamoto K., Nakayama K., Morris A., Frohman M., Kanaho Y. Phosphatidylinositol 4-phosphate 5-kinase a is α downstream effector of the small G protein ARF6 in membrane ruffl e formation. Cell 1999, 99:521-532.
179. Zhang Q., Calafat J., Janssen H., Greenberg S. ARF6 is required for growth factor-and rac-mediated membrane ruffl ing in macrophages at a stage distal to rac membrane ruffl ing. Mol Cell Biol 1999, 19:8158-8168.
180. Cichowski K., Brugge J., Brass L. Thrombin receptor activation and integrin engagement stimulate tyrosine phosphorylation of the proto-oncogene product, p95vav, in platelets. J Biol Chem 1996, 271:7544-7550.
181. Fischer K.-D., Kong Y.-Y., Nishina H., Tedford K., Marengere L., Kozieradzki I., Sasaki T., Starr M., Chan G., Garderer S., Nghiem M., Bouchard D., Barbacid M., Bernstein A., Penninger J. Vav is a regulator of cytoskeletal reorganization mediated by the T-cell receptor. Curr Biol 1998, 8:554-562.
182. Abe K., Rossman K., Liu B., Ritola K., Chiang D., Campbell S., Burridge K., Der C. Vav2 is an activator of cdc42, rac1, and rhoA. J Biol Chem 2000, 275:10141-10149.
183. Azuma T., Witke W., Stossel T., Hartwig J., Kwiatkowski D. Gelsolin is a downstream effector of rac for fi broblast motility. EMBO J 1998, 17:1362-1370.
184. Falet H., Chang G., Brohard-Bohn B., Rendu F., Hartwig J. Integrin aIIbb3 signals lead Cofilin to accelerate platelet actin dynamics. Am J Physiol Cell Physiol 2005, 289:C819-C825.
185. 2+. Biochem J 1994, 301:41-47.
186. Burridge K., Fath K. Focal contacts: Transmembrane links between the extracellular matrix and the cytoskeleton. Bioessays 1989, 10(4):104-108.
187. Burridge K., Nuckolls G., Otey C., Pavalko F., Simon K., Turner C. Actin-membrane interaction in focal adhesions. Cell Differ Dev 1990, 32(3):337-342.
188. Burridge K., Mangeat P. An interaction between vinculin and talin 1984, 308:744-746.
189. Pavalko F., Otey C., Burridge K. Identification of a filamin isoform enriched at the ends of stress fi bers in chicken embryo fi broblasts. J Cell Sci 1989, 94:109-118.
190. Turner C.E., Kramarcy N., Sealock R., Burridge K. Localization of paxillin, a focal adhesion protein, to smooth muscle dense plaques, and the myotendinous and neuromuscular junctions of skeletal muscle. Exp Cell Res 1991, 192(2):651-655.
191. Pavalko F.M., Otey C.A., Simon K.O., Burridge K. Alpha-actinin: A direct link between actin and integrins. Biochem Soc Trans 1991, 19(4):1065-1069.
192. Nakamura F., Huang L., Pestonjamasp K., Luna E., Furthmayr H. Regulation of F-actin binding to platelet moesin in vitro by both phosphorylation of threonine 558 and polyphosphatidylinositides. Mol Biol Cell 1999, 10:2669-2685.
193. Nachmias V., Golla R. Vinculin in relation to stress fi bers in spread platelets. Cell Motil Cytoskel 1991, 20:190-202.
194. Haimovich B., Regan C., DiFazio L., Ginalis E., Ji P., Purohit U., Rowley R., Bolen J., Greco R. The FcγRII receptor triggers pp125FAK phosphorylation in platelets. J Biol Chem 1996, 271:16332-16337.
195. Huang M.-M., Lipfert L., Cunningham M., Brugge J., Ginsberg M., Shattil S. Adhesive ligand binding to integrin αIIbβ3 stimulates tyrosine phosphorylation of novel protein substrates before phosphorylation of pp125FAK. J Biol Chem 1993, 122:473-483.
196. Lipfert L., Haimovich B., Schaller M., Cobb B., Parsons J., Brugge J. Integrin-dependent phosphorylation and activation of the protein tyrosine kinase pp125FAK in platelets. J Cell Biol 1992, 119:905-912.
197. Rankin S., Rozengurt E. Platelet-derived growth factor modulation of focal adhesion kinase (p125FAK) and paxillin tyrosine phosphorylation in Swiss 3T3 cells. J Biol Chem 1994, 269:704-710.
198. Grondin P., Plantavid M., Sultan C., Breton M., Mauco G., Chap H. Interaction of pp60c-src, phospholipase C, inositol-lipid, and diacylglycerol kinases with the cytoskeleton of thrombin-stimulated platelets. J Biol Chem 1991, 266:15705-15709.
199. Horvath A., Muszbek L., Kellie S. Translocation of pp60c-src to the cytoskeleton during platelet aggregation. EMBO J 1992, 11:855-861.
200. Meng F., Lowell C. A β1 integrin signaling pathway involving src-family kinases, Cbl and PI-3 kinase is required for macrophage spreading and migration. EMBO J 1998, 17:4391-4403.
201. Wu H., Reynolds A., Kanner S., Vines R., Parsons J. Identification and characterization of a novel cytoskeleton-associated pp60src substrate. Mol Cell Biol 1991, 11:5113-5124.
202. Jackson S., Schoenwaelder S., Yuan Y., Rabinowitz I., Salem H., Mitchell C. Adhesion receptor activation of phosphatidylinositol 3-kinase. Von Willebrand factor stimulates the cytoskeletal association and activation of phosphatidylinositol 3-kinase andpp60c-src in human platelets. J Biol Chem 1994, 269:27093-27099.
203. Niederman R., Pollard T. Human platelet myosin II. In vitro assembly and structure of myosin filaments. J Cell Biol 1975, 67:72-92.
204. Nachmias V.T. Reversible association of myosin with the platelet cytoskeleton. Nature 1985, 313:70-72.
205. Essler M., Amano M., Kruse H.-J., Kaibuchi K., Weber P., Aepfelbacher M. Thrombin inactivates myosin light chain phosphatase via rho and its target rho kinase in human endothelial cells. J Biol Chem 1998, 273:21867-21874.
206. Klages B., Brandt U., Simon M., Schultz G., Offermanns S. Activation of G12/G13 results in shape change and rho/rho kinase-mediated myosin light chain phosphorylation in mouse platelets. J Cell Biol 1999, 144:745-754.
207. Bernard J., Soulier J. Sur une nouvelle variété de dystrophie thrombocytaire hemorragique congenitale. Semaine des Hopitaux de Paris 1948, 24:3217-3223.
208. McGill M., Jamieson G., Drouin J., Cho M., Rock G. Morphometric analysis of platelets in Bernard-Soulier syndrome: Size and confi guration in patients and carriers. Thromb Haemost 1984, 52:37-41.
209. Berndt M., Gregory C., Chong B., Zola H., Castaldi P. Additional glycoprotein defects in Bernard-Soulier's syndrome: Confi rmation of genetic basis by parental analysis. Blood 1983, 62:800-807.
210. Clemetson K., McGregor J., James E., Dechavanne M., Luscher E. Characterization of the platelet membrane glycoprotein abnormalities in Bernard-Soulier syndrome and comparison with normal by surface-labeling techniques and high-resolution two-dimensional gel electrophoresis. J Clin Invest 1982, 70:304-311.
211. Devine D., Currie M., Rosse W., Greenberg C. Pseudo-Bernard-Soulier syndrome: Thrombocytopenia caused by autoantibody to platelet glycoprotein Ib. Blood 1987, 70:428-431.
212. Drouin J., McGregor J., Parmentier S., Izaguirre C., Clemetson K. Residual amounts of glycoprotein Ib concomitant with near-absence of glycoprotein IX in platelets of Bernard-Soulier patients. Blood 1988, 72:1086-1088.
213. Ludlow L., Schick B., Budarf M., Driscoll D., Zackai E., Cohen A., Konkle B. Indentifi cation of a mutation in the GATA binding site of the platelet glycoprotein Ibβ promoter resulting in the Bernard-Soulier syndrome. J Biol Chem 1996, 271:22076-22080.
214. Marco L., Mazzucato M., Fabris F., Roia D., Coser P., Girolami A., Vicente V., Ruggeri Z. Variant Bernard-Soulier syndrome type bolzano. Blood 1990, 86:25-31.
215. Ware J., Russell S., Ruggeri Z. Generation and rescue of a murine model of platelet dysfunction: The Bernard-Soulier syndrome. Proc Natl Acad Sci USA 2000, 97:2803-2808.
216. Ware J., Russell S., Vicente V., Scharf R., Tomer A., McMillan R., Ruggeri Z. Nonsense mutation in the glycoprotein Ibα coding sequence associated with Bernard-Soulier syndrome. Proc Natl Acad Sci USA 1990, 87:2026-2030.
217. Kunishima S., Miura H., Fukutani H., et al. Bernard-Soulier Kagoshima: Ser444 > stop mutation of the glycoprotein (gp) Ib alpha and surface expression of gpIb beta and gpIX. Blood 1994, 84:3356-3362.
218. Lanza F., Morales M., de la Salle C., Cazenave J.-P., Clemetson K., Shimomura T., Phillips D. Cloning and characterization of the gene encoding the human platelet glycoprotein V. A member of the leucine-rich glycoprotein family cleaved during thrombin-induced platelet activation. J Biol Chem 1993, 268:20801-20807.
219. Hegglin R. Gleichzeitige Konstilutionelle veranderungen an neutrophilen and thrombocyten. Helv Med Acta 1945, 12:439-440.
220. May R. Leukozyteneinschlusse. Deusch Arch Klin Med 1909, 96:439-440.
221. Consortium T.M.H.F.S. Mutations in MYH9 result in the May-Hegglin anomaly, and Fechtner and Sebastian syndromes. Nat Genet 2000, 26:103-105.
222. Kelley M., Jawien W., Ortel T., Korczak J. Mutation of MYH9, encoding non-muscle myosin heavy chain A, in May-Hegglin anomaly. Nat Genet 2000, 26:106-108.
223. Kunishima S., Kojima T., Matsushita T., Tanaka T., Tsunusawa M., Furukawa Y., Nakamura Y., Okamura T., Amemiya N., Nakayama T., Siato H. Mutations in the NMMHC-A gene cause autosomal dominant macrothrombocytopenia with leukocyte inclusions (May-Hegglin anomaly/Sebastian syndrome). Blood 2001, 97:1147-1149.