메뉴 건너뛰기




Volumn 20, Issue 14, 2000, Pages 5184-5195

The docking protein HEF1 is an apoptotic mediator at focal adhesion sites

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE; DOCKING PROTEIN; FOCAL ADHESION KINASE; HUMAN ENHANCER OF FILAMENTATION 1; LACTACYSTIN; N ACETYLLEUCYLLEUCYLNORLEUCINAL; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PROTEASOME; STRESS ACTIVATED PROTEIN KINASE; UNCLASSIFIED DRUG;

EID: 0033934340     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.20.14.5184-5195.2000     Document Type: Article
Times cited : (79)

References (87)
  • 1
    • 0029766101 scopus 로고    scopus 로고
    • Coordinate activation of c-Src by SH3- and SH2-binding sites on a novel, p130Cas-related protein
    • Alexandropoulos, K., and D. Baltimore. 1996. Coordinate activation of c-Src by SH3- and SH2-binding sites on a novel, p130Cas-related protein, Sin. Genes Dev. 10:1341-1355.
    • (1996) Sin. Genes Dev. , vol.10 , pp. 1341-1355
    • Alexandropoulos, K.1    Baltimore, D.2
  • 2
    • 0030023846 scopus 로고    scopus 로고
    • Cleavage of retinoblastoma protein during apoptosis: An interleukin 1 beta-converting enzyme-like protease as candidate
    • An, B., and Q. P. Dou. 1996. Cleavage of retinoblastoma protein during apoptosis: an interleukin 1 beta-converting enzyme-like protease as candidate. Cancer Res. 56:438-442.
    • (1996) Cancer Res. , vol.56 , pp. 438-442
    • An, B.1    Dou, Q.P.2
  • 3
    • 0032575714 scopus 로고    scopus 로고
    • Death receptors: Signaling and modulation
    • Ashkenazi, A., and V. M. Dixit. 1998. Death receptors: signaling and modulation. Science 281:1305-1308.
    • (1998) Science , vol.281 , pp. 1305-1308
    • Ashkenazi, A.1    Dixit, V.M.2
  • 4
    • 0031416275 scopus 로고    scopus 로고
    • Association of the Cas-like molecule HEF1 with CrkL following integrin and antigen receptor signaling in B cells. Possible relevance to neoplastic lymphohematopoietic cells
    • Astier, A., S. N. Manie, S. F. Law, T. Canty, N. Hagheyeghi, B. J. Druker, R. Salgia, E. A. Golemis, and A. S. Freedman. 1997. Association of the Cas-like molecule HEF1 with CrkL following integrin and antigen receptor signaling in B cells. Possible relevance to neoplastic lymphohematopoietic cells. Leuk. Lymphoma 28:65-72.
    • (1997) Leuk. Lymphoma , vol.28 , pp. 65-72
    • Astier, A.1    Manie, S.N.2    Law, S.F.3    Canty, T.4    Hagheyeghi, N.5    Druker, B.J.6    Salgia, R.7    Golemis, E.A.8    Freedman, A.S.9
  • 5
    • 0032567463 scopus 로고    scopus 로고
    • Bacterial lipopolysaccharide disrupts endothelial monolayer integrity and survival signaling events through caspase cleavage of adherens junction proteins
    • Bannerman, D. D., M. Sathyamoorthy, and S. E. Goldblum. 1998. Bacterial lipopolysaccharide disrupts endothelial monolayer integrity and survival signaling events through caspase cleavage of adherens junction proteins. J. Biol. Chem. 273:35371-35380.
    • (1998) J. Biol. Chem. , vol.273 , pp. 35371-35380
    • Bannerman, D.D.1    Sathyamoorthy, M.2    Goldblum, S.E.3
  • 6
    • 0033591228 scopus 로고    scopus 로고
    • Adaptor proteins Grb2 and Crk couple Pyk2 with activation of specific mitogen-activated protein kinase cascades
    • Blaukat, A., I. Ivankovic-Dikic, E. Gronroos, F. Dolfi, G. Tokiwa, K. Vuori, and I. Dikic. 1999. Adaptor proteins Grb2 and Crk couple Pyk2 with activation of specific mitogen-activated protein kinase cascades. J. Biol. Chem. 274:14893-14901.
    • (1999) J. Biol. Chem. , vol.274 , pp. 14893-14901
    • Blaukat, A.1    Ivankovic-Dikic, I.2    Gronroos, E.3    Dolfi, F.4    Tokiwa, G.5    Vuori, K.6    Dikic, I.7
  • 7
    • 0028927484 scopus 로고
    • Suppression of ICE and apoptosis in mammary epithelial cells by extracellular matrix
    • Boudreau, N., C. J. Sympson, Z. Werb, and M. J. Bissell. 1995. Suppression of ICE and apoptosis in mammary epithelial cells by extracellular matrix. Science 267:891-893.
    • (1995) Science , vol.267 , pp. 891-893
    • Boudreau, N.1    Sympson, C.J.2    Werb, Z.3    Bissell, M.J.4
  • 8
    • 0033551699 scopus 로고    scopus 로고
    • Role of poly(ADP-ribose) polymerase (PARP) cleavage in apoptosis. Caspase 3-resistant PARP mutant increases rates of apoptosis in transfected cells
    • Boulares, A. H., A. G. Yakovlev, V. Ivanova, B. A. Stoica, G. Wang, S. Iyer, and M. Smulson. 1999. Role of poly(ADP-ribose) polymerase (PARP) cleavage in apoptosis. Caspase 3-resistant PARP mutant increases rates of apoptosis in transfected cells. J. Biol. Chem. 274:22932-22940.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22932-22940
    • Boulares, A.H.1    Yakovlev, A.G.2    Ivanova, V.3    Stoica, B.A.4    Wang, G.5    Iyer, S.6    Smulson, M.7
  • 9
    • 0028788309 scopus 로고
    • Microfilament reorganization during apoptosis: The role of Gas2, a possible substrate for ICE-like proteases
    • Brancolini, C., M. Benedetti, and C. Schneider. 1995. Microfilament reorganization during apoptosis: the role of Gas2, a possible substrate for ICE-like proteases. EMBO J. 14:5179-5190.
    • (1995) EMBO J. , vol.14 , pp. 5179-5190
    • Brancolini, C.1    Benedetti, M.2    Schneider, C.3
  • 10
    • 0030707519 scopus 로고    scopus 로고
    • Dismantling cell-cell contacts during apoptosis is coupled to a caspase-dependent proteolytic cleavage of beta-catenin
    • Brancolini, C., D. Lazarevic, J. Rodriguez, and C. Schneider. 1997. Dismantling cell-cell contacts during apoptosis is coupled to a caspase-dependent proteolytic cleavage of beta-catenin. J. Cell Biol. 139:759-771.
    • (1997) J. Cell Biol. , vol.139 , pp. 759-771
    • Brancolini, C.1    Lazarevic, D.2    Rodriguez, J.3    Schneider, C.4
  • 11
    • 0034684997 scopus 로고    scopus 로고
    • BCAR1, a human homologue of the adapter protein p130Cas, and antiestrogen resistance in breast cancer cells
    • Brinkman, A., S. van Der Flier, E. M. Kok, and L. C. Dorssers. 2000. BCAR1, a human homologue of the adapter protein p130Cas, and antiestrogen resistance in breast cancer cells. J. Natl. Cancer Inst. 92:112-120.
    • (2000) J. Natl. Cancer Inst. , vol.92 , pp. 112-120
    • Brinkman, A.1    Van Der Flier, S.2    Kok, E.M.3    Dorssers, L.C.4
  • 12
    • 0031817916 scopus 로고    scopus 로고
    • The adenomatous polyposis coli protein and retinoblastoma protein are cleaved early in apoptosis and are potential substrates for caspases
    • Browne, S. J., M. MacFarlane, G. M. Cohen, and C. Paraskeva. 1998. The adenomatous polyposis coli protein and retinoblastoma protein are cleaved early in apoptosis and are potential substrates for caspases. Cell Death Differ. 5:206-213.
    • (1998) Cell Death Differ. , vol.5 , pp. 206-213
    • Browne, S.J.1    MacFarlane, M.2    Cohen, G.M.3    Paraskeva, C.4
  • 13
  • 14
    • 0030755579 scopus 로고    scopus 로고
    • The regulation of anoikis: MEKK-1 activation requires cleavage by caspases
    • Cardone, M. H., G. S. Salvesen, C. Widmann, G. Johnson, and S. M. Frisch. 1997. The regulation of anoikis: MEKK-1 activation requires cleavage by caspases. Cell 90:315-323.
    • (1997) Cell , vol.90 , pp. 315-323
    • Cardone, M.H.1    Salvesen, G.S.2    Widmann, C.3    Johnson, G.4    Frisch, S.M.5
  • 15
    • 0023130372 scopus 로고
    • Evaluation of a tetrazolium-based semiautomated colorimetric assay: Assessment of chemosensitivity testing
    • Carmichael, J., W. G. DeGraff, A. F. Gazdar, J. D. Minna, and J. B. Mitchell. 1987. Evaluation of a tetrazolium-based semiautomated colorimetric assay: assessment of chemosensitivity testing. Cancer Res. 47:936-942.
    • (1987) Cancer Res. , vol.47 , pp. 936-942
    • Carmichael, J.1    DeGraff, W.G.2    Gazdar, A.F.3    Minna, J.D.4    Mitchell, J.B.5
  • 16
    • 0032509565 scopus 로고    scopus 로고
    • Identification of p130Cas as a mediator of focal adhesion kinase-promoted cell migration
    • Gary, L. A., D. C. Han, T. R. Polte, S. K. Hanks, and J.-L. Guan. 1998. Identification of p130Cas as a mediator of focal adhesion kinase-promoted cell migration. J. Cell Biol. 140:211-221.
    • (1998) J. Cell Biol. , vol.140 , pp. 211-221
    • Gary, L.A.1    Han, D.C.2    Polte, T.R.3    Hanks, S.K.4    Guan, J.-L.5
  • 17
    • 0029890823 scopus 로고    scopus 로고
    • Apopain/CPP32 cleaves proteins that are essential for cellular repair: A fundamental principle of apoptotic death
    • Casciola-Rosen, L., D. W. Nicholson, T. Chong, K. R. Rowan, N. A. Thornberry, D. K. Miller, and A. Rosen. 1996. Apopain/CPP32 cleaves proteins that are essential for cellular repair: a fundamental principle of apoptotic death. J. Exp. Med. 183:1957-1964.
    • (1996) J. Exp. Med. , vol.183 , pp. 1957-1964
    • Casciola-Rosen, L.1    Nicholson, D.W.2    Chong, T.3    Rowan, K.R.4    Thornberry, N.A.5    Miller, D.K.6    Rosen, A.7
  • 18
    • 0033516655 scopus 로고    scopus 로고
    • Activation of the c-Jun N-terminal kinase/stress-activated protein kinase pathway by over-expression of caspase-8 and its homologs
    • Chaudhary, P. M., M. T. Eby, A. Jasmin, and L. Hood. 1999. Activation of the c-Jun N-terminal kinase/stress-activated protein kinase pathway by over-expression of caspase-8 and its homologs. J. Biol. Chem. 274:19211-19219.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19211-19219
    • Chaudhary, P.M.1    Eby, M.T.2    Jasmin, A.3    Hood, L.4
  • 19
    • 0032825266 scopus 로고    scopus 로고
    • Regulation of cell contraction and membrane ruffling by distinct signals in migratory cells
    • Cheresh, D. A., J. Leng, and R. L. Klemke. 1999. Regulation of cell contraction and membrane ruffling by distinct signals in migratory cells. J. Cell Biol. 146:1107-1116.
    • (1999) J. Cell Biol. , vol.146 , pp. 1107-1116
    • Cheresh, D.A.1    Leng, J.2    Klemke, R.L.3
  • 20
    • 0033046706 scopus 로고    scopus 로고
    • MEKK1 interacts with alpha-actinin and localizes to stress fibers and focal adhesions
    • Christerson, L. B., C. A. Vanderbilt, and M. H. Cobb. 1999. MEKK1 interacts with alpha-actinin and localizes to stress fibers and focal adhesions. Cell Motil. Cytoskel. 43:186-198.
    • (1999) Cell Motil. Cytoskel. , vol.43 , pp. 186-198
    • Christerson, L.B.1    Vanderbilt, C.A.2    Cobb, M.H.3
  • 21
    • 0028329953 scopus 로고
    • JNK1: A protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the cJun activation domain
    • Derijard, B., M. Hibi, I. H. Wu, T. Barrett, B. Su, T. Deng, M. Karin, and R. J. Davis. 1994. JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the cJun activation domain. Cell 76:1025-1037.
    • (1994) Cell , vol.76 , pp. 1025-1037
    • Derijard, B.1    Hibi, M.2    Wu, I.H.3    Barrett, T.4    Su, B.5    Deng, T.6    Karin, M.7    Davis, R.J.8
  • 23
    • 0033573874 scopus 로고    scopus 로고
    • Activation of caspase 3 in HL-60 cells exposed to hydrogen peroxide
    • DiPietrantonio, A. M., T. Hsieh, and J. M. Wu. 1999. Activation of caspase 3 in HL-60 cells exposed to hydrogen peroxide. Biochem. Biophys. Res. Commun. 255:477-482.
    • (1999) Biochem. Biophys. Res. Commun. , vol.255 , pp. 477-482
    • DiPietrantonio, A.M.1    Hsieh, T.2    Wu, J.M.3
  • 26
    • 0028057613 scopus 로고
    • Disruption of epithelial cell-matrix interactions induces apoptosis
    • Frisch, S. M., and H. Francis. 1994. Disruption of epithelial cell-matrix interactions induces apoptosis. J. Cell Biol. 124:619-626.
    • (1994) J. Cell Biol. , vol.124 , pp. 619-626
    • Frisch, S.M.1    Francis, H.2
  • 27
    • 0029739950 scopus 로고    scopus 로고
    • Control of adhesion-dependent cell survival by focal adhesion kinase
    • Frisch, S. M., K. Vuori, E. Ruoslahti, and P.-Y. Chan-Hui. 1996. Control of adhesion-dependent cell survival by focal adhesion kinase. J. Cell Biol. 134: 793-799.
    • (1996) J. Cell Biol. , vol.134 , pp. 793-799
    • Frisch, S.M.1    Vuori, K.2    Ruoslahti, E.3    Chan-Hui, P.-Y.4
  • 28
    • 0032479435 scopus 로고    scopus 로고
    • Caspases cleave focal adhesion kinase during apoptosis to generate a FRNK-like polypeptide
    • Gervais, F. G., N. A. Thornberry, S. C. Ruffolo, D. W. Nicholson, and S. Roy. 1998. Caspases cleave focal adhesion kinase during apoptosis to generate a FRNK-like polypeptide. J. Biol. Chem. 273:17102-17108.
    • (1998) J. Biol. Chem. , vol.273 , pp. 17102-17108
    • Gervais, F.G.1    Thornberry, N.A.2    Ruffolo, S.C.3    Nicholson, D.W.4    Roy, S.5
  • 29
    • 0032563286 scopus 로고    scopus 로고
    • Cleavage of CDK inhibitor p21(Cip1/Waf1) by caspases is an early event during DNA damage-induced apoptosis
    • Gervais, J. L., P. Seth, and H. Zhang. 1998. Cleavage of CDK inhibitor p21(Cip1/Waf1) by caspases is an early event during DNA damage-induced apoptosis. J. Biol. Chem. 273:19207-19212.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19207-19212
    • Gervais, J.L.1    Seth, P.2    Zhang, H.3
  • 32
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green, D. R., and J. C. Reed. 1998. Mitochondria and apoptosis. Science 281:1309-1312.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 33
    • 0033989562 scopus 로고    scopus 로고
    • ei24, a p53 response gene involved in growth suppression and apoptosis
    • Gu, Z., C. Flemington, T. Chittenden, and G. P. Zambetti. 2000. ei24, a p53 response gene involved in growth suppression and apoptosis. Mol. Cell. Biol. 20:233-241.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 233-241
    • Gu, Z.1    Flemington, C.2    Chittenden, T.3    Zambetti, G.P.4
  • 34
    • 0029763211 scopus 로고    scopus 로고
    • DNA-dependent protein kinase is a target for a CPP32-like apoptotic protease
    • Han, Z., N. Malik, T. Carter, W. H. Reeves, J. H. Wyche, and E. A. Hendrickson. 1996. DNA-dependent protein kinase is a target for a CPP32-like apoptotic protease. J. Biol. Chem. 271:25035-25040.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25035-25040
    • Han, Z.1    Malik, N.2    Carter, T.3    Reeves, W.H.4    Wyche, J.H.5    Hendrickson, E.A.6
  • 36
    • 0031856380 scopus 로고    scopus 로고
    • Involvement of proteasomes in migration and matrix metalloproteinase-9 production of oral squamous cell carcinoma
    • Ikebe, T., H. Takeuchi, E. Jimi, M. Beppu, M. Shinohara, and K. Shirasuna. 1998. Involvement of proteasomes in migration and matrix metalloproteinase-9 production of oral squamous cell carcinoma. Int. J. Cancer 77:578-585.
    • (1998) Int. J. Cancer , vol.77 , pp. 578-585
    • Ikebe, T.1    Takeuchi, H.2    Jimi, E.3    Beppu, M.4    Shinohara, M.5    Shirasuna, K.6
  • 37
    • 0032054723 scopus 로고    scopus 로고
    • Signal transduction by the c-Jun N-terminal kinase (JNK) - From inflammation to development
    • Ip, Y. T., and R. J. Davis. 1998. Signal transduction by the c-Jun N-terminal kinase (JNK) - from inflammation to development. Curr. Opin. Cell Biol. 10:205-219.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 205-219
    • Ip, Y.T.1    Davis, R.J.2
  • 38
    • 0029562687 scopus 로고
    • Molecular cloning of a cDNA encoding a phosphoprotein, Efs, which contains a Src homology 3 domain and associates with Fyn
    • Ishino, M., T. Ohba, H. Sasaki, and T. Sasaki. 1995. Molecular cloning of a cDNA encoding a phosphoprotein, Efs, which contains a Src homology 3 domain and associates with Fyn. Oncogene 11:2331-2338.
    • (1995) Oncogene , vol.11 , pp. 2331-2338
    • Ishino, M.1    Ohba, T.2    Sasaki, H.3    Sasaki, T.4
  • 39
    • 0040298568 scopus 로고    scopus 로고
    • Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis
    • Janicke, R. U., M. L. Sprengart, M. R. Wati, and A. G. Porter. 1998. Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis. J. Biol. Chem. 273:9357-9360.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9357-9360
    • Janicke, R.U.1    Sprengart, M.L.2    Wati, M.R.3    Porter, A.G.4
  • 40
    • 0030462563 scopus 로고    scopus 로고
    • Specific cleavage of the retinoblastoma protein by an ICE-like protease in apoptosis
    • Janicke, R. U., P. A. Walker, X. Y. Un, and A. G. Porter. 1996. Specific cleavage of the retinoblastoma protein by an ICE-like protease in apoptosis. EMBO J. 15:6969-6978.
    • (1996) EMBO J. , vol.15 , pp. 6969-6978
    • Janicke, R.U.1    Walker, P.A.2    Un, X.Y.3    Porter, A.G.4
  • 41
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr, J. F., A. H. Wyllie, and A. R. Currie. 1972. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer 26:239-257.
    • (1972) Br. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 42
    • 0029011805 scopus 로고
    • Cell cycle and apoptosis: Common pathways to life and death
    • King, K. L., and J. A. Cidlowski. 1995. Cell cycle and apoptosis: common pathways to life and death. J. Cell. Biochem. 58:175-180.
    • (1995) J. Cell. Biochem. , vol.58 , pp. 175-180
    • King, K.L.1    Cidlowski, J.A.2
  • 43
    • 0032559562 scopus 로고    scopus 로고
    • CAS/Crk coupling serves as a "molecular switch" for induction of cell migration
    • Klemke, R. L., J. Leng, R. Molander, P. C. Brooks, K. Vuori, and D. A. Cheresh. 1998. CAS/Crk coupling serves as a "molecular switch" for induction of cell migration. J. Cell Biol. 140:961-972.
    • (1998) J. Cell Biol. , vol.140 , pp. 961-972
    • Klemke, R.L.1    Leng, J.2    Molander, R.3    Brooks, P.C.4    Vuori, K.5    Cheresh, D.A.6
  • 45
    • 0029891787 scopus 로고    scopus 로고
    • cas-like docking protein, associates with focal adhesion kinase and induces pseudohyphal growth in Saccharomyces cerevisiae
    • cas-like docking protein, associates with focal adhesion kinase and induces pseudohyphal growth in Saccharomyces cerevisiae. Mol. Cell. Biol. 16:3327-3337.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3327-3337
    • Law, S.F.1    Estojak, J.2    Wang, B.3    Mysliwiec, T.4    Kruh, G.D.5    Golemis, E.A.6
  • 46
    • 0033544003 scopus 로고    scopus 로고
    • Dimerization of the docking/adaptor protein HEF1 via a carboxy-terminal helix-loop-helix domain
    • Law, S. F., Y.-Z. Zhang, S. Fashena, G. Toby, J. Estojak, and E. A. Golemis. 1999. Dimerization of the docking/adaptor protein HEF1 via a carboxy-terminal helix-loop-helix domain. Exp. Cell Res. 252:224-235.
    • (1999) Exp. Cell Res. , vol.252 , pp. 224-235
    • Law, S.F.1    Zhang, Y.-Z.2    Fashena, S.3    Toby, G.4    Estojak, J.5    Golemis, E.A.6
  • 47
    • 0031813880 scopus 로고    scopus 로고
    • Cell-cycle regulated processing of HEF1 to multiple protein forms differentially targeted to multiple compartments
    • Law, S. F., Y.-Z. Zhang, A. Klein-Szanto, and E. A. Golemis. 1998. Cell-cycle regulated processing of HEF1 to multiple protein forms differentially targeted to multiple compartments. Mol. Cell. Biol. 18:3540-3551.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3540-3551
    • Law, S.F.1    Zhang, Y.-Z.2    Klein-Szanto, A.3    Golemis, E.A.4
  • 48
    • 0027437541 scopus 로고
    • Nuclear events of apoptosis in vitro in cell-free mitotic extracts: A model system for analysis of the active phase of apoptosis
    • Lazebnik, Y. A., S. Cole, C. A. Cooke, W. G. Nelson, and W. C. Earnshaw. 1993. Nuclear events of apoptosis in vitro in cell-free mitotic extracts: a model system for analysis of the active phase of apoptosis. J. Cell Biol. 123:7-22.
    • (1993) J. Cell Biol. , vol.123 , pp. 7-22
    • Lazebnik, Y.A.1    Cole, S.2    Cooke, C.A.3    Nelson, W.G.4    Earnshaw, W.C.5
  • 49
    • 0028102478 scopus 로고
    • Cleavage of poly(ADP-rihose) polymerase by a proteinase with properties like ICE
    • Lazebnik, Y. A., S. H. Kaufmann, S. Desnoyers, G. G. Poirier, and W. C. Earnshaw. 1994. Cleavage of poly(ADP-rihose) polymerase by a proteinase with properties like ICE. Nature 371:346-347.
    • (1994) Nature , vol.371 , pp. 346-347
    • Lazebnik, Y.A.1    Kaufmann, S.H.2    Desnoyers, S.3    Poirier, G.G.4    Earnshaw, W.C.5
  • 51
    • 0031443641 scopus 로고    scopus 로고
    • Activation of hPAK65 by caspase cleavage induces some of the morphological and biochemical changes of apoptosis
    • Lee, N., H. MacDonald, C. Reinhard, R. Halenbeck, A. Roulston, T. Shi, and L. T. Williams. 1997. Activation of hPAK65 by caspase cleavage induces some of the morphological and biochemical changes of apoptosis. Proc. Natl. Acad. Sci. USA 94:13642-13647.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13642-13647
    • Lee, N.1    MacDonald, H.2    Reinhard, C.3    Halenbeck, R.4    Roulston, A.5    Shi, T.6    Williams, L.T.7
  • 54
    • 0030298294 scopus 로고    scopus 로고
    • Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-kappaB activation prevents cell death
    • Liu, Z. G., H. Hsu, D. V. Goeddel, and M. Karin. 1996. Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-kappaB activation prevents cell death. Cell 87:565-576.
    • (1996) Cell , vol.87 , pp. 565-576
    • Liu, Z.G.1    Hsu, H.2    Goeddel, D.V.3    Karin, M.4
  • 55
    • 0033153086 scopus 로고    scopus 로고
    • The role of caspases in development, immunity, and apoptotic signal transduction: Lessons from knockout mice
    • Los, M., S. Wesselborg, and K. Schulze-Osthoff. 1999. The role of caspases in development, immunity, and apoptotic signal transduction: lessons from knockout mice. Immunity 10:629-639.
    • (1999) Immunity , vol.10 , pp. 629-639
    • Los, M.1    Wesselborg, S.2    Schulze-Osthoff, K.3
  • 56
    • 0033537975 scopus 로고    scopus 로고
    • NSP1 defines a novel family of adaptor proteins linking integrin and tyrosine kinase receptors to the c-Jun N-terminal kinase/stress-activated protein kinase signaling pathway
    • Lu, Y., J. Brush, and T. Stewart. 1999. NSP1 defines a novel family of adaptor proteins linking integrin and tyrosine kinase receptors to the c-Jun N-terminal kinase/stress-activated protein kinase signaling pathway. J. Biol. Chem. 274:10047-10052.
    • (1999) J. Biol. Chem. , vol.274 , pp. 10047-10052
    • Lu, Y.1    Brush, J.2    Stewart, T.3
  • 59
    • 0029904694 scopus 로고    scopus 로고
    • Structure and function of Cas-L, a 105-kD Crk-associated substrate-related protein that is involved in beta-1 integrin-mediated signaling in lymphocytes
    • Minegishi, M., K. Tachibana, T. Sato, S. Iwata, Y. Nojima, and C. Morimoto. 1996. Structure and function of Cas-L, a 105-kD Crk-associated substrate-related protein that is involved in beta-1 integrin-mediated signaling in lymphocytes. J. Exp. Med. 184:1365-1375.
    • (1996) J. Exp. Med. , vol.184 , pp. 1365-1375
    • Minegishi, M.1    Tachibana, K.2    Sato, T.3    Iwata, S.4    Nojima, Y.5    Morimoto, C.6
  • 60
    • 0030994236 scopus 로고    scopus 로고
    • Evidence for CPP32 activation in the absence of apoptosis during T lymphocyte stimulation
    • Miossec, C., V. Dutilleul, F. Fassy, and A. Diu-Hercend. 1997. Evidence for CPP32 activation in the absence of apoptosis during T lymphocyte stimulation. J. Biol. Chem. 272:13459-13462.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13459-13462
    • Miossec, C.1    Dutilleul, V.2    Fassy, F.3    Diu-Hercend, A.4
  • 62
    • 0032472369 scopus 로고    scopus 로고
    • The MAP kinase kinase kinase MLK2 co-localizes with activated JNK along microtubules and associates with kinesin superfamily motor KIF3
    • Nagata, K.-I., A. Puis, C. Futter, P. Aspenstrom, E. Schaefer, T. Nakata, N. Hirokawa, and A. Hall. 1998. The MAP kinase kinase kinase MLK2 co-localizes with activated JNK along microtubules and associates with kinesin superfamily motor KIF3. EMBO J. 17:149-158.
    • (1998) EMBO J. , vol.17 , pp. 149-158
    • Nagata, K.-I.1    Puis, A.2    Futter, C.3    Aspenstrom, P.4    Schaefer, E.5    Nakata, T.6    Hirokawa, N.7    Hall, A.8
  • 63
    • 0029034873 scopus 로고
    • Integrin-mediated cell adhesion promotes tyrosine phosphorylation of p130Cas, a Src homology 3-containing molecule having multiple Src homology 2-binding motifs
    • Nojima, Y., N. Morino, T. Mimura, K. Hamasaki, H. Furuya, R. Sakai, T. Sato, K. Tachibana, C. Morimoto, Y. Yazaki, and H. Hirai. 1995. Integrin-mediated cell adhesion promotes tyrosine phosphorylation of p130Cas, a Src homology 3-containing molecule having multiple Src homology 2-binding motifs. J. Biol. Chem. 270:15398-15402.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15398-15402
    • Nojima, Y.1    Morino, N.2    Mimura, T.3    Hamasaki, K.4    Furuya, H.5    Sakai, R.6    Sato, T.7    Tachibana, K.8    Morimoto, C.9    Yazaki, Y.10    Hirai, H.11
  • 64
    • 0033214510 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of Crk-associated substrate lymphocyte-type is a critical element in TCR- and beta1 integrin-induced T lymphocyte migration
    • Ohashi, Y., S. Iwata, K. Kamiguchi, and C. Morimoto. 1999. Tyrosine phosphorylation of Crk-associated substrate lymphocyte-type is a critical element in TCR- and beta1 integrin-induced T lymphocyte migration. J. Immunol. 163:3727-3734.
    • (1999) J. Immunol. , vol.163 , pp. 3727-3734
    • Ohashi, Y.1    Iwata, S.2    Kamiguchi, K.3    Morimoto, C.4
  • 65
    • 0032513128 scopus 로고    scopus 로고
    • T cell receptor-mediated tyrosine phosphorylation of Cas-L, a 105-kDa Crk-associated substrate-related protein, and its association of Crk and C3G
    • Ohashi, Y., K. Tachibana, K. Kamiguchi, H. Fujita, and C. Morimoto. 1998. T cell receptor-mediated tyrosine phosphorylation of Cas-L, a 105-kDa Crk-associated substrate-related protein, and its association of Crk and C3G. J. Biol. Chem. 273:6446-6451
    • (1998) J. Biol. Chem. , vol.273 , pp. 6446-6451
    • Ohashi, Y.1    Tachibana, K.2    Kamiguchi, K.3    Fujita, H.4    Morimoto, C.5
  • 66
    • 0032505029 scopus 로고    scopus 로고
    • Dot far-Western blot analysis of relative binding affinities of the src homology 3 domains of efs and its related proteins
    • Ohba, T, M. Ishino, H. Aoto, and T. Sasaki. 1998. Dot far-Western blot analysis of relative binding affinities of the src homology 3 domains of efs and its related proteins. Anal. Biochem. 262:185-192.
    • (1998) Anal. Biochem. , vol.262 , pp. 185-192
    • Ohba, T.1    Ishino, M.2    Aoto, H.3    Sasaki, T.4
  • 67
    • 0034160011 scopus 로고    scopus 로고
    • Integrin signaling: A new Cas(t) of characters enters the stage
    • O'Neill, G. M., S. J. Fashena, and E. A. Golemis. 2000. Integrin signaling: a new Cas(t) of characters enters the stage. Trends Cell Biol. 10:111-119.
    • (2000) Trends Cell Biol. , vol.10 , pp. 111-119
    • O'Neill, G.M.1    Fashena, S.J.2    Golemis, E.A.3
  • 68
    • 0032919345 scopus 로고    scopus 로고
    • The role of the ubiquitin-proteasome pathway in apoptosis
    • Orlowski, R. Z. 1999. The role of the ubiquitin-proteasome pathway in apoptosis. Cell Death Differ. 6:303-313.
    • (1999) Cell Death Differ. , vol.6 , pp. 303-313
    • Orlowski, R.Z.1
  • 69
    • 0032055973 scopus 로고    scopus 로고
    • Neuronal cell death
    • Pettmann, B., and C. E. Henderson. 1998. Neuronal cell death. Neuron 20:633-647.
    • (1998) Neuron , vol.20 , pp. 633-647
    • Pettmann, B.1    Henderson, C.E.2
  • 70
    • 0030918572 scopus 로고    scopus 로고
    • Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2
    • Rudel, T., and G. M. Bokoch. 1997. Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2. Science 276:1571-1574.
    • (1997) Science , vol.276 , pp. 1571-1574
    • Rudel, T.1    Bokoch, G.M.2
  • 71
    • 0027990414 scopus 로고
    • A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner
    • Sakai, R., A. Iwamatsu, N. Hirano, S. Ogawa, T. Tanaka, H. Mano, Y. Yazaki, and H. Hirai. 1994. A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner. EMBO J. 13:3748-3756.
    • (1994) EMBO J. , vol.13 , pp. 3748-3756
    • Sakai, R.1    Iwamatsu, A.2    Hirano, N.3    Ogawa, S.4    Tanaka, T.5    Mano, H.6    Yazaki, Y.7    Hirai, H.8
  • 72
    • 0034052103 scopus 로고    scopus 로고
    • Chat, a Cas/HEF1-associated adaptor protein that integrates multiple signaling pathways
    • Sakakibara, A., and S. Hattori. 2000. Chat, a Cas/HEF1-associated adaptor protein that integrates multiple signaling pathways. J. Biol. Chem. 275:6404-6410.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6404-6410
    • Sakakibara, A.1    Hattori, S.2
  • 73
    • 0030611712 scopus 로고    scopus 로고
    • Differential signaling after beta1 integrin ligation is mediated through binding of CRKL to p120CBL and p110HEF1
    • Sattler, M., R. Salgia, G. Shrikhande, S. Verma, N. Uemura, S. F. Law, E. A. Golemis, and J. D. Griffin. 1997. Differential signaling after beta1 integrin ligation is mediated through binding of CRKL to p120CBL and p110HEF1. J. Biol. Chem. 272:14320-14326.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14320-14326
    • Sattler, M.1    Salgia, R.2    Shrikhande, G.3    Verma, S.4    Uemura, N.5    Law, S.F.6    Golemis, E.A.7    Griffin, J.D.8
  • 75
    • 0032577703 scopus 로고    scopus 로고
    • Transient poly(ADP-ribosyl)ation of nuclear proteins and role of poly(ADP-ribose) polymerase in the early stages of apoptosis
    • Simbulan-Rosenthal, C. M., D. S. Rosenthal, S. Iyer, A. H. Boulares, and M. E. Smulson. 1998. Transient poly(ADP-ribosyl)ation of nuclear proteins and role of poly(ADP-ribose) polymerase in the early stages of apoptosis. J. Biol. Chem. 273:13703-13712.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13703-13712
    • Simbulan-Rosenthal, C.M.1    Rosenthal, D.S.2    Iyer, S.3    Boulares, A.H.4    Smulson, M.E.5
  • 77
    • 0030669961 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of crk-associated substrates by focal adhesion kinase. A putative mechanism for the integrin-mediated tyrosine phosphorylation of crk-associated substrates
    • Tachibana, K., T. Urano, H. Fujita, Y. Ohashi, K. Kamiguchi, S. Iwata, H. Hirai, and C. Morimoto. 1997. Tyrosine phosphorylation of crk-associated substrates by focal adhesion kinase. A putative mechanism for the integrin-mediated tyrosine phosphorylation of crk-associated substrates. J. Biol. Chem. 272:29083-29090.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29083-29090
    • Tachibana, K.1    Urano, T.2    Fujita, H.3    Ohashi, Y.4    Kamiguchi, K.5    Iwata, S.6    Hirai, H.7    Morimoto, C.8
  • 79
    • 0029102383 scopus 로고
    • CrmA-inhibitable cleavage of the 70-kDa protein component of the U1 small nuclear ribonucleoprotein during Fas- and tumor necrosis factor-induced apoptosis
    • Tewari, M., D. R. Beidler, and V. M. Dixit. 1995. CrmA-inhibitable cleavage of the 70-kDa protein component of the U1 small nuclear ribonucleoprotein during Fas- and tumor necrosis factor-induced apoptosis. J. Biol. Chem. 270:18738-18741.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18738-18741
    • Tewari, M.1    Beidler, D.R.2    Dixit, V.M.3
  • 80
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thomberry, N. A., and Y. Lazebnik. 1998. Caspases: enemies within. Science 281:1312-1316.
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thomberry, N.A.1    Lazebnik, Y.2
  • 81
    • 0027236043 scopus 로고
    • B-cell apoptosis induced by antigen receptor crosslinking is blocked by a T-cell signal through CD40
    • Tsubata, T., J. Wu, and T. Honjo. 1993. B-cell apoptosis induced by antigen receptor crosslinking is blocked by a T-cell signal through CD40. Nature 364:645-648.
    • (1993) Nature , vol.364 , pp. 645-648
    • Tsubata, T.1    Wu, J.2    Honjo, T.3
  • 82
    • 0032525138 scopus 로고    scopus 로고
    • Identification of BCAR3 by a random search for genes involved in antiestrogen resistance of human breast cancer cells
    • van Agthoven, T., T. L. van Agthoven, A. Dekker, P. J. van der Spek, L. Vreede, and L. C. Dorssers. 1998. Identification of BCAR3 by a random search for genes involved in antiestrogen resistance of human breast cancer cells. EMBO J. 17:2799-2808.
    • (1998) EMBO J. , vol.17 , pp. 2799-2808
    • Van Agthoven, T.1    Van Agthoven, T.L.2    Dekker, A.3    Van Der Spek, P.J.4    Vreede, L.5    Dorssers, L.C.6
  • 84
    • 0028981376 scopus 로고
    • Tyrosine phosphorylation of p130Cas and cortactin accompanies integrin-mediated cell adhesion to extracellular matrix
    • Vuori, K., and E. Ruoslahti. 1995. Tyrosine phosphorylation of p130Cas and cortactin accompanies integrin-mediated cell adhesion to extracellular matrix. J. Biol. Chem. 270:22259-22262.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22259-22262
    • Vuori, K.1    Ruoslahti, E.2
  • 85
    • 0029871920 scopus 로고    scopus 로고
    • Cleavage of sterol regulatory element binding proteins (SREBPs) by CPP32 during apoptosis
    • Wang, X., N. G. Zelenski, J. Yang, J. Sakai, M. S. Brown, and J. L. Goldstein. 1996. Cleavage of sterol regulatory element binding proteins (SREBPs) by CPP32 during apoptosis. EMBO J. 15:1012-1020.
    • (1996) EMBO J. , vol.15 , pp. 1012-1020
    • Wang, X.1    Zelenski, N.G.2    Yang, J.3    Sakai, J.4    Brown, M.S.5    Goldstein, J.L.6
  • 86
    • 0032975430 scopus 로고    scopus 로고
    • Possible involvement of caspase-like family in maintenance of cytoskeleton integrity
    • Watanabe, Y., and T. Akaike. 1999. Possible involvement of caspase-like family in maintenance of cytoskeleton integrity. J. Cell. Physiol. 179:45-51.
    • (1999) J. Cell. Physiol. , vol.179 , pp. 45-51
    • Watanabe, Y.1    Akaike, T.2
  • 87


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.