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Volumn 16, Issue 8, 2005, Pages 3511-3520

Impaired Akt activity down-modulation, caspase-3 activation, and apoptosis in cells expressing a caspase-resistant mutant of RasGAP at position 157

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 3; CISPLATIN; COMPLEMENTARY DNA; FAS LIGAND; PROTEIN KINASE B; RAS PROTEIN; STAUROSPORINE;

EID: 23044488799     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E05-01-0080     Document Type: Article
Times cited : (35)

References (37)
  • 2
    • 10744233396 scopus 로고    scopus 로고
    • Terminal differentiation of human epidermal keratinocytes involves mitochondria- and caspase-dependent cell death pathway
    • Allombert-Blaise, C. et al. (2003). Terminal differentiation of human epidermal keratinocytes involves mitochondria- and caspase-dependent cell death pathway. Cell Death Differ. 20, 850-852.
    • (2003) Cell Death Differ. , vol.20 , pp. 850-852
    • Allombert-Blaise, C.1
  • 3
    • 3042733029 scopus 로고    scopus 로고
    • RasGTPase-activating protein is a target of caspases in spontaneous apoptosis of lung carcinoma cells and in response to etoposide
    • Bartling, B., Yang, J. Y., Michod, D., Widmann, C., Lewensohn, R., and Zhivotovsky, B. (2004). RasGTPase-activating protein is a target of caspases in spontaneous apoptosis of lung carcinoma cells and in response to etoposide. Carcinogenesis 25, 909-921.
    • (2004) Carcinogenesis , vol.25 , pp. 909-921
    • Bartling, B.1    Yang, J.Y.2    Michod, D.3    Widmann, C.4    Lewensohn, R.5    Zhivotovsky, B.6
  • 4
    • 0036829593 scopus 로고    scopus 로고
    • Proteolytic activation of protein kinase C-epsilon by caspase-mediated processing and transduction of antiapoptotic signals
    • Basu, A., Lu, D., Sun, B., Moor, A. N., Akkaraju, G. R., and Huang, J. (2002). Proteolytic activation of protein kinase C-epsilon by caspase-mediated processing and transduction of antiapoptotic signals. J. Biol. Chem. 277, 41850-41856.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41850-41856
    • Basu, A.1    Lu, D.2    Sun, B.3    Moor, A.N.4    Akkaraju, G.R.5    Huang, J.6
  • 6
    • 0037468853 scopus 로고    scopus 로고
    • Apoptotic pathway and MAPKs differentially regulate chemotropic responses of retinal growth cones
    • Campbell, D. S., and Holt, C. E. (2003). Apoptotic pathway and MAPKs differentially regulate chemotropic responses of retinal growth cones. Neuron 37, 939-952.
    • (2003) Neuron , vol.37 , pp. 939-952
    • Campbell, D.S.1    Holt, C.E.2
  • 8
    • 0842281645 scopus 로고    scopus 로고
    • Cell death: Critical control points
    • Danial, N. N., and Korsmeyer, S. J. (2004). Cell death: critical control points. Cell 116, 205-219.
    • (2004) Cell , vol.116 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 10
  • 12
    • 0242432345 scopus 로고    scopus 로고
    • Many cuts to ruin: A comprehensive update of caspase substrates
    • Fischer, U., Janicke, R. U., and Schulze-Osthoff, K. (2003). Many cuts to ruin: a comprehensive update of caspase substrates. Cell Death Differ. 10, 76-100.
    • (2003) Cell Death Differ. , vol.10 , pp. 76-100
    • Fischer, U.1    Janicke, R.U.2    Schulze-Osthoff, K.3
  • 13
    • 0030976895 scopus 로고    scopus 로고
    • A sequential two-step mechanism for the production of the mature p17, p12 form of caspase-3 in vitro
    • Man, Z., Hendrickson, E. A., Bremner, T. A., and Wyche, J. H. (1997). A sequential two-step mechanism for the production of the mature p17, p12 form of caspase-3 in vitro. J. Biol. Chem. 272, 13432-13436.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13432-13436
    • Man, Z.1    Hendrickson, E.A.2    Bremner, T.A.3    Wyche, J.H.4
  • 14
    • 0037315457 scopus 로고    scopus 로고
    • Two adjacent trimeric Fas ligands are required for Fas signaling and formation of a death-inducing signaling complex
    • Holler, N. et al. (2003). Two adjacent trimeric Fas ligands are required for Fas signaling and formation of a death-inducing signaling complex. Mol. Cell. Biol. 23, 1428-1440.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 1428-1440
    • Holler, N.1
  • 15
    • 0029991350 scopus 로고    scopus 로고
    • Transfecting mammalian cells: Optimization of critical parameters affecting calcium-phosphate precipitate formation
    • Jordan, M., Schallhorn, A., and Wurm, F. M. (1996). Transfecting mammalian cells: optimization of critical parameters affecting calcium-phosphate precipitate formation. Nucleic Acids Res. 24, 596-601.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 596-601
    • Jordan, M.1    Schallhorn, A.2    Wurm, F.M.3
  • 17
    • 0031811884 scopus 로고    scopus 로고
    • Ras-GAP controls Rhomediated cytoskeletal reorganization through its SH3 domain
    • Leblanc, V., Tocque, B., and Delumeau, I. (1998). Ras-GAP controls Rhomediated cytoskeletal reorganization through its SH3 domain. Mol. Cell. Biol. 18, 5567-5578.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5567-5578
    • Leblanc, V.1    Tocque, B.2    Delumeau, I.3
  • 18
    • 0037389275 scopus 로고    scopus 로고
    • The p54 cleaved form of the tyrosine kinase Lyn generated by caspases during BCR-induced cell death in B lymphoma acts as a negative regulator of apoptosis
    • Luciano, F., Herrant, M., Jacquel, A., Ricci, J. E., and Auberger, P. (2003). The p54 cleaved form of the tyrosine kinase Lyn generated by caspases during BCR-induced cell death in B lymphoma acts as a negative regulator of apoptosis. FASEB J. 27, 711-713.
    • (2003) FASEB J. , vol.27 , pp. 711-713
    • Luciano, F.1    Herrant, M.2    Jacquel, A.3    Ricci, J.E.4    Auberger, P.5
  • 19
    • 10644271655 scopus 로고    scopus 로고
    • A RasGAP-derived cell permeable peptide potently enhances genotoxin-induced cytotoxicity in tumor cells
    • Michod, D., Yang, J. Y., Chen, J., Bonny, C., and Widmann, C. (2004). A RasGAP-derived cell permeable peptide potently enhances genotoxin-induced cytotoxicity in tumor cells. Oncogene 23, 8971-8978.
    • (2004) Oncogene , vol.23 , pp. 8971-8978
    • Michod, D.1    Yang, J.Y.2    Chen, J.3    Bonny, C.4    Widmann, C.5
  • 20
    • 0037380579 scopus 로고    scopus 로고
    • Caspases signal not only apoptosis but also antigen-induced activation in cells of the immune system
    • Newton, K., and Strasser, A. (2003). Caspases signal not only apoptosis but also antigen-induced activation in cells of the immune system. Genes Dev. 27, 819-825.
    • (2003) Genes Dev. , vol.27 , pp. 819-825
    • Newton, K.1    Strasser, A.2
  • 21
    • 0032785021 scopus 로고    scopus 로고
    • Caspase structure, proteolytic substrates, and function during apoptotic cell death
    • Nicholson, D. W. (1999). Caspase structure, proteolytic substrates, and function during apoptotic cell death. Cell Death Differ. 6, 1028-1042.
    • (1999) Cell Death Differ. , vol.6 , pp. 1028-1042
    • Nicholson, D.W.1
  • 23
    • 0037155827 scopus 로고    scopus 로고
    • Apoptosis stimulated by the 91-kDa caspase cleavage MEKK1 fragment requires rranslocation to soluble cellular compartments
    • Schlesinger, T. K., Bonvin, C., Jarpe, M. B., Fanger, G. R., Cardinaux, J.-R., Johnson, G. L., and Widmann, C. (2002). Apoptosis stimulated by the 91-kDa caspase cleavage MEKK1 fragment requires rranslocation to soluble cellular compartments. J. Biol. Chem. 277, 10283-10291.
    • (2002) J. Biol. Chem. , vol.277 , pp. 10283-10291
    • Schlesinger, T.K.1    Bonvin, C.2    Jarpe, M.B.3    Fanger, G.R.4    Cardinaux, J.-R.5    Johnson, G.L.6    Widmann, C.7
  • 24
    • 0035831473 scopus 로고    scopus 로고
    • Executioner caspase-3, -6, and -7 perform distinct, non-redundant roles during the demolition phase of apoptosis
    • Slee, E. A., Adrain, C., and Martin, S. J. (2001). Executioner caspase-3, -6, and -7 perform distinct, non-redundant roles during the demolition phase of apoptosis. J. Biol. Chem. 276, 7320-7326.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7320-7326
    • Slee, E.A.1    Adrain, C.2    Martin, S.J.3
  • 25
    • 0035282570 scopus 로고    scopus 로고
    • A conserved XIAP-interaction motif in caspase-9 and Smac/DIABLO regulates caspase activity and apoptosis
    • Srinivasula, S. M. et al. (2001). A conserved XIAP-interaction motif in caspase-9 and Smac/DIABLO regulates caspase activity and apoptosis. Nature 410, 112-116.
    • (2001) Nature , vol.410 , pp. 112-116
    • Srinivasula, S.M.1
  • 26
    • 0032416062 scopus 로고    scopus 로고
    • Death by a thousand cuts: An ever increasing list of caspase substrates
    • Stroh, C., and Schulze-Osthoff, K. (1998). Death by a thousand cuts: an ever increasing list of caspase substrates. Cell Death Differ. 5, 997-1000.
    • (1998) Cell Death Differ. , vol.5 , pp. 997-1000
    • Stroh, C.1    Schulze-Osthoff, K.2
  • 27
    • 3142704153 scopus 로고    scopus 로고
    • Delayed neutrophil apoptosis in sepsis is associated with maintenance of mitochondrial transmembrane potential and reduced caspase-9 activity
    • Taneja, R., Parodo, J., Jia, S. H., Kapus, A., Rotstein, O. D., and Marshall, J. C. (2004). Delayed neutrophil apoptosis in sepsis is associated with maintenance of mitochondrial transmembrane potential and reduced caspase-9 activity. Crit. Care Med. 32, 1460-1469.
    • (2004) Crit. Care Med. , vol.32 , pp. 1460-1469
    • Taneja, R.1    Parodo, J.2    Jia, S.H.3    Kapus, A.4    Rotstein, O.D.5    Marshall, J.C.6
  • 28
    • 0030701607 scopus 로고    scopus 로고
    • Fas induces cytoplasmic apoptoric responses and activation of the MKK7-JNK/SAPK and MKK6-p38 pathways independent of CPP32-like proteases
    • Toyoshima, F., Moriguchi, T., and Nishida, E. (1997). Fas induces cytoplasmic apoptoric responses and activation of the MKK7-JNK/SAPK and MKK6-p38 pathways independent of CPP32-like proteases. J. Cell Biol. 139, 1005-1015.
    • (1997) J. Cell Biol. , vol.139 , pp. 1005-1015
    • Toyoshima, F.1    Moriguchi, T.2    Nishida, E.3
  • 29
    • 0028989013 scopus 로고
    • The GTPase-acrivating protein of ras suppresses platelet-derived growth factor β receptor signaling by silencing phospholipase c-γ1
    • Valius, M., Secrist, J., and Kazlauskas, A. (1995). The GTPase-acrivating protein of ras suppresses platelet-derived growth factor β receptor signaling by silencing phospholipase c-γ1. Mol. Cell. Biol. 15, 3058-3071.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3058-3071
    • Valius, M.1    Secrist, J.2    Kazlauskas, A.3
  • 30
    • 0030899808 scopus 로고    scopus 로고
    • Aberrant Ras regulation and reduced p190 tyrosine phosphorylation in cells lacking p120-Gap
    • Van der Geer, P., Henkemeyer, M., Jacks, T., and Pawson, T. (1997). Aberrant Ras regulation and reduced p190 tyrosine phosphorylation in cells lacking p120-Gap. Mol. Cell. Biol. 17, 1840-1847.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1840-1847
    • Van Der Geer, P.1    Henkemeyer, M.2    Jacks, T.3    Pawson, T.4
  • 32
    • 0031785812 scopus 로고    scopus 로고
    • Proteolytic cleavage of Ras GTPase-activating protein during apoptosis
    • Wen, L. P., Madani, K., Martin, G. A., and Rosen, G. D. (1998). Proteolytic cleavage of Ras GTPase-activating protein during apoptosis. Cell Death Differ. 5, 729-734.
    • (1998) Cell Death Differ. , vol.5 , pp. 729-734
    • Wen, L.P.1    Madani, K.2    Martin, G.A.3    Rosen, G.D.4
  • 33
    • 0029117847 scopus 로고
    • Agonist-induced internalization and recycling of the glucagon-like peptide-1 receptor in transfected fibroblasts and in insulinomas
    • Widmann, C., Dolci, W., and Thorens, B. (1995). Agonist-induced internalization and recycling of the glucagon-like peptide-1 receptor in transfected fibroblasts and in insulinomas. Biochem. J. 310, 203-214.
    • (1995) Biochem. J. , vol.310 , pp. 203-214
    • Widmann, C.1    Dolci, W.2    Thorens, B.3
  • 34
    • 8644273229 scopus 로고    scopus 로고
    • Partial cleavage of RasGAP by caspases is required for cell survival in mild stress conditions
    • Yang, J.-Y., Michod, D., Walicki, J., Murphy, B. M., Kasibhatla, S., Martin, S., and Widmann, C. (2004). Partial cleavage of RasGAP by caspases is required for cell survival in mild stress conditions. Mol. Cell. Biol. 24, 10425-10436.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 10425-10436
    • Yang, J.-Y.1    Michod, D.2    Walicki, J.3    Murphy, B.M.4    Kasibhatla, S.5    Martin, S.6    Widmann, C.7
  • 35
    • 0034928845 scopus 로고    scopus 로고
    • Antiapoptotic signaling generated by caspase-induced cleavage of RasGAP
    • Yang, J.-Y., and Widmann, C. (2001). Antiapoptotic signaling generated by caspase-induced cleavage of RasGAP. Mol. Cell. Biol. 21, 5346-5358.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5346-5358
    • Yang, J.-Y.1    Widmann, C.2
  • 36
    • 0037177856 scopus 로고    scopus 로고
    • The RasGAP N-terminal fragment generated by caspase cleavage protects cells in a Ras/PI3K/Akt-dependent manner that does not rely on NFκB activation
    • Yang, J.-Y., and Widmann, C. (2002). The RasGAP N-terminal fragment generated by caspase cleavage protects cells in a Ras/PI3K/Akt-dependent manner that does not rely on NFκB activation. J. Biol. Chem. 277, 14641-14646.
    • (2002) J. Biol. Chem. , vol.277 , pp. 14641-14646
    • Yang, J.-Y.1    Widmann, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.