Critical roles for the actin cytoskeleton and cdc42 in regulating platelet integrin α₂β₁

References

• Shattil SJ, Newman PJ. Integrins: Dynamic scaffolds for adhesion and signaling in platelets. Blood 2004; 104: 1606–1615
   PubMed Web of Science ®Google Scholar
• Humphries MJ. Integrin structure. Biochem Soc Trans 2000; 28: 311–339
   PubMed Web of Science ®Google Scholar
• Ginsberg MH, Partridge A, Shattil SJ. Integrin regulation. Curr Opin Cell Biol 2005; 17: 509–516
   PubMed Web of Science ®Google Scholar
• Carman CV, Springer TA. Integrin avidity regulation: Are changes in affinity and conformation underemphasized?. Curr Opin Cell Biol 2003; 15: 547–556
   PubMed Web of Science ®Google Scholar
• Nieswandt B, Watson SP. Platelet-collagen interaction: Is GPVI the central receptor?. Blood 2003; 102: 449–461
   PubMed Web of Science ®Google Scholar
• Santoro SA, Zutter MM. The α2β1 integrin: a collagen receptor on platelets and other cells. Thromb Haemost 1995; 74: 813–821
   PubMed Web of Science ®Google Scholar
• Chen H, Kahn ML. Reciprocal signaling by integrin and nonintegrin receptors during collagen activation of platelets. Mol Cell Biol 2003; 23: 4764–4777
   PubMed Web of Science ®Google Scholar
• Lecut C, Schoolmeester A, Kuijpers MJE, Broers JLV, van Zandvoort MAMJ, Vanhoorelbeke K, et al. Principal role of glycoprotein VI in α2β1 and αIIbβ3 activation during collagen-induced thrombus formation. Arterioscler Thromb Vasc Biol 2004; 24: 1727–1733
   PubMed Web of Science ®Google Scholar
• Sarratt KL, Chen H, Zutter MM, Santoro SA, Hammer DA, Kahn ML. GPVI and α2β1 play independent critical roles during platelet adhesion and aggregate formation to collagen under flow. Blood 2005; 106: 1268–1277
   PubMed Web of Science ®Google Scholar
• Bernardi B, Guidetti GF, Campus F, Crittenden JR, Graybiel AM, Balduini C, et al. The small GTPase Rap1b regulates the cross talk between platelet integrin α2β1 and integrin αIIbβ3. Blood 2006; 107: 2728–2735
   PubMed Web of Science ®Google Scholar
• Van de Walle GR, Schoolmeester A, Iserbyt BF, Cosemans JMEM, Heemskerk JWM, Hoylaerts MF, et al. Activation of αIIbβ3 is a sufficient but also an imperative prerequisite for activation of α2β1on platelets. Blood 2007; 109: 595–602
   PubMed Web of Science ®Google Scholar
• Diaz-Ricart M, Arderiu G, Estebanell E, Perez-Pujol S, Lozano M, White JG, et al. Inhibition of cytoskeletal assembly by cytochalasin B prevents signaling through tyrosine phosphorylation and secretion triggered by collagen but not by thrombin. Am J Pathol 2002; 160: 329–337
   PubMed Web of Science ®Google Scholar
• Nakano T, Hanasaki K, Arita H. Possible involvement of cytoskeleton in collagen-stimulated activation of phospholipases in human platelets. J Biol Chem 1989; 264: 5400–5406
   PubMed Web of Science ®Google Scholar
• Nobes CD, Hall A. Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 1995; 81: 53–62
   PubMed Web of Science ®Google Scholar
• Soulet C, Gendreau S, Missy K, Benard V, Plantavid M, Payrastre B. Characterisation of Rac activation in thrombin- and collagen-stimulated human blood platelets. FEBS Letters 2001; 507: 253–258
   PubMed Web of Science ®Google Scholar
• Pula G, Schuh K, Nakayama K, Nakayama KI, Walter U, Poole AW. PKCδ regulates collagen-induced platelet aggregation through inhibition of VASP-mediated filopodia formation. Blood 2006; 108: 4035–4044
   PubMed Web of Science ®Google Scholar
• Ridley AJ, Schwartz MA, Burridge K, Firtel RA, Ginsberg MH, Borisy G, et al. Cell migration: Integrating signals from front to back. Science 2003; 302: 1704–1709
   PubMed Web of Science ®Google Scholar
• Wood W, Martin P. Structures in focus–filopodia. Int J Biochem Cell Biol 2002; 34: 726–730
   PubMed Web of Science ®Google Scholar
• Mould AP, Askari JA, Barton S, Kline AD, McEwan PA, Craig SE, et al. Integrin activation involves a conformational change in the alpha 1 helix of the beta subunit A-domain. J Biol Chem 2002; 277: 19800–19805
   PubMed Web of Science ®Google Scholar
• Humphries JD, Schofield NR, Mostafavi-Pour Z, Green LJ, Garratt AN, Mould AP, et al. Dual functionality of the anti-{beta}1 integrin antibody, 12G10, exemplifies agonistic signalling from the ligand binding pocket of integrin adhesion receptors. J Biol Chem 2005; 280: 10234–10243
   PubMed Web of Science ®Google Scholar
• Pula G, Crosby D, Baker J, Poole AW. Functional interaction of protein kinase Cα with the tyrosine kinases Syk and Src in human platelets. J Biol Chem 2005; 280: 7194–7205
   PubMed Web of Science ®Google Scholar
• DeMali KA, Wennerberg K, Burridge K. Integrin signaling to the actin cytoskeleton. Curr Opin Cell Biol 2003; 15: 572–582
   PubMed Web of Science ®Google Scholar
• Wiesner S, Legate KR, Fassler R. Integrin-actin interactions. Cell Mol Life Sci 2005; 62: 1081–1099
   PubMed Web of Science ®Google Scholar
• Vidal C, Geny B, Melle J, Jandrot-Perrus M, Fontenay-Roupie M. Cdc42/Rac1-dependent activation of the p21-activated kinase (PAK) regulates human platelet lamellipodia spreading: Implication of the cortical-actin binding protein cortactin. Blood 2002; 100: 4462–4469
   PubMed Web of Science ®Google Scholar
• Wonerow P, Pearce AC, Vaux DJ, Watson SP. A Critical Role for Phospholipase Cγ2 in αIIbβ3-mediated Platelet Spreading. J Biol Chem 2003; 278: 37520–37529
   PubMed Web of Science ®Google Scholar
• Jung SM, Moroi M. Activation of the platelet collagen receptor integrin α2β1: Its mechanism and participation in the physiological functions of platelets. Trends Cardiovasc Med 2000; 10: 285–292
   PubMed Web of Science ®Google Scholar
• Inoue K, Ozaki Y, Satoh K, Wu Y, Yatomi Y, Shin Y, et al. Signal transduction pathways mediated by glycoprotein Ia/IIa in human platelets: Comparison with those of Glycoprotein VI. Biochem Biophys Res Commun 1999; 256: 114–120
   PubMed Web of Science ®Google Scholar
• Bergmeier W, Bouvard D, Eble JA, Mokhtari-Nejad R, Schulte V, Zirngibl H, et al. Rhodocytin (aggretin) activates platelets lacking α2β1 integrin, glycoprotein VI, and the ligand-binding domain of glycoprotein Ibα. J Biol Chem 2001; 276: 25121–25126
   PubMed Web of Science ®Google Scholar
• Eble JA, Beermann B, Hinz HJ, Schmidt-Hederich A. α2β1 integrin is not recognized by rhodocytin but is the specific, high affinity target of rhodocetin, an RGD-independent disintegrin and potent inhibitor of cell adhesion to collagen. J Biol Chem 2001; 276: 12274–12284
   PubMed Web of Science ®Google Scholar
• Suzuki-Inoue K, Fuller GLJ, Garcia A, Eble JA, Pohlmann S, Inoue O, et al. A novel Syk-dependent mechanism of platelet activation by the C-type lectin receptor CLEC-2. Blood 2006; 107: 542–549
   PubMed Web of Science ®Google Scholar
• McCarty OJT, Larson MK, Auger JM, Kalia N, Atkinson BT, Pearce AC, et al. Rac1 is essential for platelet lamellipodia formation and aggregate stability under flow. J Biol Chem 2005; 280: 39474–39484
   PubMed Web of Science ®Google Scholar
• Nieswandt B, Brakebusch C, Bergmeier W, Schulte V, Bouvard D, Mokhtari-Nejad R, et al. Glycoprotein VI but not alpha2beta1 integrin is essential for platelet interaction with collagen. EMBO J 2001; 20: 2120–2130
   PubMed Web of Science ®Google Scholar
• Hers I, Berlanga O, Tiekstra MJ, Kamiguti AS, Theakston RD, Watson SP. Evidence against a direct role of the integrin α2β1 in collagen-induced tyrosine phosphorylation in human platelets. Eur J Biochem 2000; 267: 2088–2097
   PubMedGoogle Scholar
• Schoolmeester A, Vanhoorelbeke K, Katsutani S, Depraetere H, Feys HB, Heemskerk JMW, et al. Monoclonal antibody IAC-1 is specific for activated α2β1 and binds to amino acids 199 to 201 of the integrin α2 I-domain. Blood 2004; 104: 390–396
   PubMed Web of Science ®Google Scholar