Sequential Regulation of the Small GTPase Rap1 in Human Platelets

REFERENCES

• Alig, L., Edenhofer, A., Hadvary, P., Huerzeler, M., Knopp, D., Mueller, M., Steiner, B., Trzeciak, A., and Weller, T.. 1992. Low molecular weight, non-peptide fibrinogen receptor antagonists. J. Med. Chem. 35:4393–4407
   PubMed Web of Science ®Google Scholar
• Altschuler, D. L., Peterson, S. N., Ostrowski, M. C., and Lapetina, E. C.. 1995. Cyclic AMP-dependent activation of Rap1b. J. Biol. Chem. 270:10373–10376
   PubMedGoogle Scholar
• Bochetti, D., Fantin, G., and Doni, M. G.. 1984. Influence of the pure synthetic PAF (platelet aggregating factor) on clot retraction and platelet aggregation. Scand. J. Haematol. 32:33–40
   PubMedGoogle Scholar
• Bos, J. L.. 1998. All in the family?—new insights and questions regarding interconnectivity of Ras, Rap, and Ral. EMBO J. 17:6776–6782
   PubMed Web of Science ®Google Scholar
• Calvete, J. J.. 1994. Clues for understanding the structure and function of a prototypical human integrin: the platelet glycoprotein IIb/IIIa complex. Thromb. Haemostasis 72:1–15
   PubMed Web of Science ®Google Scholar
• Chenevert, J., Corrado, K., Bender, A., Pringle, J. R., and Herskowitz, I.. 1992. A yeast gene (BEM1) necessary for cell polarization whose product contains two SH3 domains. Nature 356:77–79
   PubMedGoogle Scholar
• de Rooij, J., Zwartkruis, F. J. T., Verheijen, M. H. G., Cool, R. H., Nijman, S. M. B., Wittinghofer, A., and Bos, J. L.. 1998. Epac is a Rap1 guanine nucleotide-exchange factor directly activated by cyclic AMP. Nature 396:474–477
   PubMed Web of Science ®Google Scholar
• Fischer, T. H., Gatling, M. N., McCormick, F., Duffy, C. M., White, G. C.II.. 1994. Incorporation of Rap 1b into the platelet cytoskeleton is dependent on thrombin activation and extracellular calcium. J. Biol. Chem. 269:17257–17261
   PubMedGoogle Scholar
• Franke, B., Akkerman, J. W. N., and Bos, J. L.. 1997. Rapid Ca2+-mediated activation of Rap1 in human platelets. EMBO J. 16:252–259
   PubMed Web of Science ®Google Scholar
• Frelinger, A. L.III, Du, X., Plow, E. F., and Ginsberg, M. H.. 1991. Monoclonal antibodies to ligand-occupied conformers of integrin αIIbβ3 (glycoprotein IIb-IIIa) alter receptor affinity, specificity, and function. J. Biol. Chem. 266:17106–17111
   PubMed Web of Science ®Google Scholar
• Gotoh, T., Hattori, S., Nakamura, S., Kitayama, H., Noda, M., Takai, Y., Kaibuchi, K., Matsui, H., Hatase, O., Takahasi, H., Kurata, T., and Matsuda, M.. 1995. Identification of Rap1 as a target for the Crk SH3 domain-binding guanine nucleotide-releasing factor C3G. Mol. Cell. Biol. 15:6746–6753
   PubMed Web of Science ®Google Scholar
• Hacking, C. M., Huigsloot, M., Pladet, M. W., Nieuwenhuis, H. K., van Rijn, H. J., and Akkerman, J. W. N.. 1999. Low-density lipoprotein enhances platelet secretion via integrin-αIIbβ3-mediated signaling. Arterioscler. Thromb. Vasc. Biol. 19:239–247
   PubMedGoogle Scholar
• Kawasaki, H., Springett, G. M., Toki, S., Canales, J. J., Harlan, P., Blumenstiel, J. P., Chen, E. J., Bany, A., Mochizuki, N., Ashbacher, A., Matsuda, M., Housman, D. E., and Graybiel, A. M.. 1998. A Rap guanine nucleotide exchange factor enriched highly in the basal ganglia. Proc. Natl. Acad. Sci. USA 95:13278–13283
   PubMed Web of Science ®Google Scholar
• Kawasaki, H., Springett, G. M., Mochizuki, N., Toki, S., Nakaya, M., Matsuda, M., Housman, D. E., and Graybiel, A. M.. 1998. A family of cAMP-binding proteins that directly activate RAP1. Science 282:2275–2279
   PubMed Web of Science ®Google Scholar
• Kitayama, H., Sugimoto, Y., Matsuzaki, T., Ikawa, Y., and Noda, M.. 1989. A RAS-related gene with transformation suppressor activity. Cell 56:77–84
   PubMed Web of Science ®Google Scholar
• Kiyokawa, E., Mochizuki, N., Kurata, T., and Matsuda, M.. 1997. Role of Crk oncogene product in physiologic signaling. Crit. Rev. Oncog. 8:329–342
   PubMedGoogle Scholar
• McLeod, S. J., Ingham, R. J., Bos, J. L., Kurosaki, T., and Gold, M.. 1998. Activation of the Rap1 GTPase by the B cell antigen receptor. J. Biol. Chem. 273:29218–29223
   PubMed Web of Science ®Google Scholar
• M'Rabet, L., Coffer, P., Zwartkruis, F., Franke, B., Koenderman, L., and Bos, J. L.. 1998. Activation of Rap1 in human neutrophils. Blood 92:2133–2140
   PubMed Web of Science ®Google Scholar
• Noda, M.. 1993. Structures and functions of the Krev-1 transformation suppressor and its relatives. Biophys. Biochim. Acta 1155:95–105
   Google Scholar
• Park, H. O., Chant, J., and Herskowitz, I.. 1993. BUD2 encodes a GTPase-activating protein for Bud1/Rsr1 necessary for proper bud-site selection in yeast. Nature 365:269–274
   PubMedGoogle Scholar
• Park, H. O., Bi, E., Pringle, J. R., and Herskowitz, I.. 1997. Two active states of the Ras-related Bud1/Rsr1 protein bind to different effectors to determine yeast cell polarity. Proc. Natl. Acad. Sci. USA 94:4463–4468
   PubMedGoogle Scholar
• Phillips, D. R., Charo, L. F., and Scarborough, R. M.. 1991. GPIIb-IIIa: the responsive integrin. Cell 65:359–362
   PubMed Web of Science ®Google Scholar
• Posern, G., Weber, C. K., Rapp, U. R., and Feller, S. M.. 1998. Activity of Rap1 is regulated by bombesin, cell adhesion, and cell density in NIH3T3 fibroblasts. J. Biol. Chem. 273:24297–24300
   PubMedGoogle Scholar
• Reedquist, K. A., and Bos, J. L.. 1998. Costimulation through CD28 suppresses T cell receptor-dependent activation of the Ras-like small GTPase Rap1 in human T lymphocytes. J. Biol. Chem. 273:4944–4949
   PubMed Web of Science ®Google Scholar
• Schlegel, N., Gayet, O., Morel-Kopp, M. C., Wyler, B., Hurtaud-Roux, M. F., Kaplan, C., and McGregor, J.. 1995. The molecular genetic basis of Glanzmann's thrombasthenia in a gypsy population in France: identification of a new mutation on the alpha IIb gene. Blood 86:977–982
   PubMed Web of Science ®Google Scholar
• Torti, M., and Lapetina, E. G.. 1994. Structure and function of Rap proteins in human platelets. Thromb. Haemostasis 71:533–543
   PubMedGoogle Scholar
• Tsukamoto, N., Hattori, M., Yang, H., Bos, J. L., and Minato, N.. 1999. Rap1 GTPase-activating protein SPA-1 negatively regulates cell adhesion. J. Biol. Chem. 274:18463–18469
   PubMed Web of Science ®Google Scholar
• van den Berghe, N., Cool, R. H., Horn, G., and Wittinghofer, A.. 1997. Biochemical characterization of C3G: an exchange factor that discriminates between Rap1 and Rap2 and is not inhibited by Rap1A(S17N). Oncogene 15:845–850
   PubMedGoogle Scholar
• van Willigen, G., Hers, I., Gorter, G. G., and Akkerman, J. W. N.. 1996. Exposure of ligand-binding sites on platelet integrin αIIbβ3 by phosphorylation of the β3 subunit. Biochem. J. 314:769–779
   PubMedGoogle Scholar
• Wang, H.-Y., and Friedman, E.. 1990. Protein kinase C translocation in human platelets. Life Sci. 47:1419–1425
   PubMedGoogle Scholar
• Wolthuis, R. M. F., Franke, B., van Triest, M. H., Bauer, B., Cool, R. H., Camonis, J. H., Akkerman, J. W. N., and Bos, J. L.. 1998. Activation of the small GTPase Ral in platelets. Mol. Cell. Biol. 18:2486–2491
   PubMed Web of Science ®Google Scholar
• Zwartkruis, F. J. T., Wolthuis, R. M. F., Nabben, N. M. J. M., Franke, B., and Bos, J. L.. 1998. Extracellular signal-regulated activation of Rap1 fails to interfere in Ras effector signalling. EMBO J. 17:5905–5912
   PubMed Web of Science ®Google Scholar