Antiapoptotic Signaling Generated by Caspase-Induced Cleavage of RasGAP

REFERENCES

• Alam, A., L. Y. Cohen, S. Aouad, and R. P. Sekaly. 1999. Early activation of caspases during T lymphocyte stimulation results in selective substrate cleavage in nonapoptotic cells. J. Exp. Med. 190:1879–1890.
   PubMed Web of Science ®Google Scholar
• Barkett, M., and T. D. Gilmore. 1999. Control of apoptosis by Rel/NF-kappaB transcription factors. Oncogene 18:6910–6924.
   PubMed Web of Science ®Google Scholar
• Bar-Sagi, D., and A. Hall. 2000. Ras and Rho GTPases: a family reunion. Cell 103:227–238.
   PubMed Web of Science ®Google Scholar
• Campbell, S. L., R. Khosravi-Far, K. L. Rossman, G. J. Clark, and C. J. Der. 1998. Increasing complexity of Ras signaling. Oncogene 17:1395–1413.
   PubMed Web of Science ®Google Scholar
• Cardone, M., G. S. Salvesen, C. Widmann, G. L. Johnson, and S. M. Frisch. 1997. The regulation of anoikis: MEKK-1 activation requires cleavage by caspases. Cell 90:315–323.
   PubMed Web of Science ®Google Scholar
• Datta, R., H. Kojima, K. Yoshida, and D. Kufe. 1997. Caspase-3-mediated cleavage of protein kinase C theta in induction of apoptosis. J. Biol. Chem. 272:20317–20320.
   PubMed Web of Science ®Google Scholar
• De Maria, R., A. Zeuner, A. Eramo, C. Domenichelli, D. Bonci, F. Grignani, S. M. Srinivasula, E. S. Alnemri, U. Testa, and C. Peschle. 1999. Negative regulation of erythropoiesis by caspase-mediated cleavage of GATA-1. Nature 401:489–493.
   PubMed Web of Science ®Google Scholar
• Deveraux, Q. L., and T. C. Reed. 1999. IAP family proteins—suppressors of apoptosis. Genes Dev. 13:239–252.
   PubMed Web of Science ®Google Scholar
• Fay, P. J., T. M. Smudzin, and F. J. Walker. 1991. Activated protein C-catalyzed inactivation of human factor VIII and factor VIIIa. Identification of cleavage sites and correlation of proteolysis with cofactor activity. J. Biol. Chem. 266:20139–20145.
   PubMedGoogle Scholar
• Franke, T. F., D. R. Kaplan, and L. C. Cantley. 1997. PI3K: downstream AKTion blocks apoptosis. Cell 88:435–437.
   PubMed Web of Science ®Google Scholar
• Frisch, S. M., and H. Francis. 1994. Disruption of epithelial cell-matrix interactions induces apoptosis. J. Cell Biol. 124:619–626.
   PubMed Web of Science ®Google Scholar
• Fritz, G., and B. Kaina. 2001. Ras-related GTPase RhoB represses NF-kappa B signaling. J. Biol. Chem. 276:3115–3122.
   PubMedGoogle Scholar
• Ghayur, T., S. Banerjee, M. Hugunin, D. Butler, L. Herzog, A. Carter, L. Quintal, L. Sekut, R. Talanian, M. Paskind, W. Wong, R. Kamen, D. Tracey, and H. Allen. 1997. Caspase-1 processes IFN-gamma-inducing factor and regulates LPS-induced IFN-gamma production. Nature 386:619–623.
   PubMed Web of Science ®Google Scholar
• Henkemeyer, M., D. J. Rossi, D. P. Holmyard, M. C. Puri, G. Mbamalu, K. Harpal, T. S. Shih, T. Jacks, and T. Pawson. 1995. Vascular system defects and neuronal apoptosis in mice lacking Ras GTPase-activating protein. Nature 377:695–701.
   PubMed Web of Science ®Google Scholar
• Hu, K.-Q., and J. Settleman. 1997. Tandem SH2 binding sites mediate the RasGAP-RhoGAP interaction: a conformational mechanism for SH3 domain regulation. EMBO J. 16:473–483.
   PubMedGoogle Scholar
• Kennedy, N. J., T. Kataoka, J. Tschopp, and R. C. Budd. 1999. Caspase activation is required for T cell proliferation. J. Exp. Med. 190:1891–1896.
   PubMed Web of Science ®Google Scholar
• LaCasse, E. C., S. Baird, R. G. Korneluk, and A. E. MacKenzie. 1998. The inhibitors of apoptosis (IAPs) and their emerging role in cancer. Oncogene 17:3247–3259.
   PubMed Web of Science ®Google Scholar
• Leblanc, V., I. Delumeau, and B. Tocque. 1999. Ras-GTPase activating protein inhibition specifically induces apoptosis of tumour cells. Oncogene 18:4884–4889.
   PubMedGoogle Scholar
• Leblanc, V., B. Tocque, and I. Delumeau. 1998. Ras-GAP controls Rho-mediated cytoskeletal reorganization through its SH3 domain. Mol. Cell. Biol. 18:5567–5578.
   PubMed Web of Science ®Google Scholar
• McGlade, J., B. Brunkhorst, D. Anderson, G. Mbamalu, J. Settleman, S. Dedhar, M. Rozakis-Adcock, L. B. Chen, and T. Pawson. 1993. The N-terminal region of GAP regulates cytoskeletal structure and cell adhesion. EMBO J. 12:3073–3081.
   PubMedGoogle Scholar
• Medema, R. H., W. L. de Laat, G. A. Martin, F. McCormick, and J. L. Bos. 1992. GTPase-activating protein SH2-SH3 domains induce gene expression in a Ras-dependent fashion. Mol. Cell. Biol. 12:3425–3430.
   PubMedGoogle Scholar
• Nelson, R. M., and G. L. Long. 1989. A general method of site-specific mutagenesis using a modification of the Thermus aquaticus polymerase chain reaction. Anal. Biochem. 180:147–151.
   PubMedGoogle Scholar
• Nicholson, D. W.. 1999. Caspase structure, proteolytic substrates, and function during apoptotic cell death. Cell Death Differ. 6:1028–1042.
   PubMed Web of Science ®Google Scholar
• Tamir, I., J. C. Stolpa, C. D. Helgason, K. Nakamura, P. Bruhns, M. Daeron, and J. C. Cambier. 2000. The RasGAP-binding protein p62dok is a mediator of inhibitory FcγRIIB signals in B cells. Immunity 12:347–358.
   PubMed Web of Science ®Google Scholar
• Thornberry, N., and Y. A. Lazebnik. 1998. Caspases: enemies within. Science 281:1312–1316.
   PubMed Web of Science ®Google Scholar
• Thornberry, N. A., H. G. Bull, J. R. Calaycay, K. T. Chapman, A. D. Howard, M. J. Kostura, D. K. Miller, S. M. Molineaux, J. R. Weidner, J. Aunins, K. O. Elliston, J. M. Ayala, F. J. Casano, J. Chin, G. J. F. Ding, L. A. Egger, E. P. Gaffney, G. Limjuco, O. C. Palyha, S. M. Raju, A. M. Rolando, J. P. Salley, T.-T. Yamin, T. D. Lee, J. E. Shively, M. MacCross, R. A. Mumford, J. A. Schmidt, and M. J. Tocci. 1992. A novel heterodimeric cysteine protease is required for interleukin-1β processing in monocytes. Nature 356:768–774.
   PubMed Web of Science ®Google Scholar
• Tocque, B., I. Delumeau, F. Parker, F. Maurier, M. C. Multon, and F. Schweighoffer. 1997. Ras-GTPase activating protein (GAP): a putative effector for Ras. Cell Signal. 9:153–158.
   PubMed Web of Science ®Google Scholar
• Toyoshima, F., T. Moriguchi, and E. Nishida. 1997. Fas induces cytoplasmic apoptotic responses and activation of the MKK7-JNK/SAPK and MKK6–p38 pathways independent of CPP32-like proteases. J. Cell Biol. 139:1005–1015.
   PubMed Web of Science ®Google Scholar
• Valius, M., J. Secrist, and A. Kazlauskas. 1995. The GTPase-activating protein of ras suppresses platelet-derived growth factor β receptor signaling by silencing phospholipase c-γ1. Mol. Cell. Biol. 15:3058–3071.
   PubMed Web of Science ®Google Scholar
• van't Veer, C., N. J. Golden, M. Kalafatis, and K. G. Mann. 1997. Inhibitory mechanism of the protein C pathway on tissue factor-induced thrombin generation. Synergistic effect in combination with tissue factor pathway inhibitor. J. Biol. Chem. 272:7983–7994.
   PubMedGoogle Scholar
• Widmann, C., W. Dolci, and B. Thorens. 1995. Agonist-induced internalization and recycling of the glucagon-like peptide-1 receptor in transfected fibroblasts and in insulinomas. Biochem. J. 310:203–214.
   PubMedGoogle Scholar
• Widmann, C., P. Gerwins, N. Lassignal Johnson, M. B. Jarpe, and G. L. Johnson. 1998. MEKK1, a substrate for DEVD-directed caspases, is involved in genotoxin-induced apoptosis. Mol. Cell. Biol. 18:2416–2429.
   PubMed Web of Science ®Google Scholar
• Widmann, C., S. Gibson, and G. L. Johnson. 1998. Caspase-dependent cleavage of signaling proteins during apoptosis. A turn-off mechanism for anti-apoptotic signals. J. Biol. Chem. 273:7141–7147.
   PubMed Web of Science ®Google Scholar
• Widmann, C., N. Lassignal Johnson, A. M. Gardner, R. J. Smith, and G. L. Johnson. 1997. Potentiation of apoptosis by low dose stress stimuli in cells expressing activated MEK kinase 1. Oncogene 15:2439–2447.
   PubMed Web of Science ®Google Scholar
• Xia, Z., M. Dickens, J. Raingeaud, R. J. Davis, and M. E. Greenberg. 1995. Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis. Science 270:1326–1331.
   PubMed Web of Science ®Google Scholar
• Yamanashi, Y., T. Tamura, T. Kanamori, H. Yamane, H. Nariuchi, T. Yamamoto, and D. Baltimore. 2000. Role of the rasGAP-associated docking protein p62(dok) in negative regulation of B cell receptor-mediated signaling. Genes Dev. 14:11–16.
   PubMed Web of Science ®Google Scholar
• Zheng, T. S., S. Hunot, K. Kuida, and R. A. Flavell. 1999. Caspase knockouts: matters of life and death. Cell Death Differ. 6:1043–1053.
   PubMedGoogle Scholar