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Volumn 14, Issue 9, 2000, Pages 1083-1092

Proteolytic cleavage of phospholipase C-γ1 during apoptosis in Molt-4 cells

Author keywords

PLC 1; Proteolysis; Tyrosine phosphorylation

Indexed keywords

CASPASE; PHOSPHOLIPASE C;

EID: 0001455392     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fasebj.14.9.1083     Document Type: Article
Times cited : (70)

References (47)
  • 1
    • 0028929328 scopus 로고
    • Mechanisms and genes of cellular suicide
    • Steller, H. (1995) Mechanisms and genes of cellular suicide. Science 267, 1445-1449
    • (1995) Science , vol.267 , pp. 1445-1449
    • Steller, H.1
  • 2
    • 0022497852 scopus 로고
    • Genetic control of programmed cell death in the nematode C. Elegans
    • Ellis, H. M., and Horvitz, H. R. (1986) Genetic control of programmed cell death in the nematode C. elegans. Cell 44, 817-829
    • (1986) Cell , vol.44 , pp. 817-829
    • Ellis, H.M.1    Horvitz, H.R.2
  • 3
    • 0027525104 scopus 로고
    • The C. Elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme
    • Yuan, J., Shaham, S., Ledoux, S., Ellis, H., and Horvitz, H. R. (1993) The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme. Cell 75, 641-652
    • (1993) Cell , vol.75 , pp. 641-652
    • Yuan, J.1    Shaham, S.2    Ledoux, S.3    Ellis, H.4    Horvitz, H.R.5
  • 5
    • 0030931876 scopus 로고    scopus 로고
    • Caspases: The executioners of apoptosis
    • Cohen, G. M. (1997) Caspases: the executioners of apoptosis. Biochem. J. 326, 1-16
    • (1997) Biochem. J. , vol.326 , pp. 1-16
    • Cohen, G.M.1
  • 6
    • 0030702084 scopus 로고    scopus 로고
    • Caspases: Intracellular signaling by proteolysis
    • Salvesen, G. S., and Dixit, V. M. (1997) Caspases: Intracellular signaling by proteolysis. Cell 91, 443-446
    • (1997) Cell , vol.91 , pp. 443-446
    • Salvesen, G.S.1    Dixit, V.M.2
  • 7
    • 0030011398 scopus 로고    scopus 로고
    • Involvement of MACH, a novel MORTI/FADD-interacting protease, in Fas/APO-1-and TNF receptor-induced cell death
    • Boldin M. P., Goncharov T. M., Goltsev Y. V., and Wallach D. (1996) Involvement of MACH, a novel MORTI/FADD-interacting protease, in Fas/APO-1-and TNF receptor-induced cell death. Cell 85, 803-815
    • (1996) Cell , vol.85 , pp. 803-815
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3    Wallach, D.4
  • 8
    • 2642689658 scopus 로고    scopus 로고
    • Proteases to die for
    • Cryns, V., and Yuan, J. (1998) Proteases to die for. Genes Dev. 12, 1551-1570
    • (1998) Genes Dev. , vol.12 , pp. 1551-1570
    • Cryns, V.1    Yuan, J.2
  • 9
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl-2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
    • Luo, X., Budihardjo, I., Zou, H., Slaughter, C., and Wang, X. (1998) Bid, a Bcl-2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors, Cell 94, 481-490
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 10
    • 0033519705 scopus 로고    scopus 로고
    • Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
    • Shimizu, S., Narita, M., and Tsujimoto, Y. (1999) Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. Nature (London) 399, 483-487
    • (1999) Nature (London) , vol.399 , pp. 483-487
    • Shimizu, S.1    Narita, M.2    Tsujimoto, Y.3
  • 11
    • 0030745646 scopus 로고    scopus 로고
    • Apaf-1, a human protein homologous to C. Elegans CED-4, participates in cytochrome c-dependent activation of caspase-3
    • Zou, H., Henzel, W. J., Liu, X., Lutschg, A., and Wang, X. (1997) Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell 90, 405-413
    • (1997) Cell , vol.90 , pp. 405-413
    • Zou, H.1    Henzel, W.J.2    Liu, X.3    Lutschg, A.4    Wang, X.5
  • 12
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li, P., Nijhawan, D., Budihardjo, I., Srinivasula, S. M., Ahmad, M., Alnemri, E. S., and Wang, X. (1997) Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91, 479-489
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 13
    • 0030916417 scopus 로고    scopus 로고
    • DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis
    • Liu, X., Zou, H., Slaughter, C., and Wang, X. (1997) DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis. Cell 89, 175-184
    • (1997) Cell , vol.89 , pp. 175-184
    • Liu, X.1    Zou, H.2    Slaughter, C.3    Wang, X.4
  • 14
    • 0030776157 scopus 로고    scopus 로고
    • Caenorhabditis elegans CED-9 protein is a bifunctional cell-death inhibitor
    • Xue, D., and Horvitz, H. R. (1997) Caenorhabditis elegans CED-9 protein is a bifunctional cell-death inhibitor. Nature (London) 390, 305-308
    • (1997) Nature (London) , vol.390 , pp. 305-308
    • Xue, D.1    Horvitz, H.R.2
  • 17
    • 0030918572 scopus 로고    scopus 로고
    • Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2
    • Rudel, T., and Bokoch, G. M. (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
  • 19
    • 0030907987 scopus 로고    scopus 로고
    • PI3K: Downstream AKTion blocks apoptosis
    • Franke, T. F., Kaplan, D. R., and Cantley, L. C. (1997) PI3K: downstream AKTion blocks apoptosis. Cell 88, 435-437
    • (1997) Cell , vol.88 , pp. 435-437
    • Franke, T.F.1    Kaplan, D.R.2    Cantley, L.C.3
  • 20
    • 0344653108 scopus 로고    scopus 로고
    • Activation of phospholipase C.-γ by phosphatidylinositol 3,4,5-trisphosphate
    • Bae, Y. S., Cantley, L. G., Chen, C. S., Kim, S. R., Kwon, K. S., and Rhee, S. G. (1998) Activation of phospholipase C.-γ by phosphatidylinositol 3,4,5-trisphosphate. J. Biol. Chem. 273, 4465-4469
    • (1998) J. Biol. Chem. , vol.273 , pp. 4465-4469
    • Bae, Y.S.1    Cantley, L.G.2    Chen, C.S.3    Kim, S.R.4    Kwon, K.S.5    Rhee, S.G.6
  • 21
    • 0024403320 scopus 로고
    • Studies of inositol phospholipid-specific phospholipase C
    • Rhee, S. G., Suh, P.-G., Ryu, S. H., and Lee, S. Y. (1989) Studies of inositol phospholipid-specific phospholipase C. Science 244, 546-550
    • (1989) Science , vol.244 , pp. 546-550
    • Rhee, S.G.1    Suh, P.-G.2    Ryu, S.H.3    Lee, S.Y.4
  • 22
    • 0028906542 scopus 로고
    • An SH3 domain is required for the mitogenic activity of microinjected phospholipase C-γ1
    • Huang, P. S., Davis, L., Huber, H., Goodhart, P. J., Wegrzyn, R. E., Oliff, A., and Heimbrook, D. C. (1995) An SH3 domain is required for the mitogenic activity of microinjected phospholipase C-γ1. FEBS Lett. 358, 287-292
    • (1995) FEBS Lett. , vol.358 , pp. 287-292
    • Huang, P.S.1    Davis, L.2    Huber, H.3    Goodhart, P.J.4    Wegrzyn, R.E.5    Oliff, A.6    Heimbrook, D.C.7
  • 23
    • 15644368498 scopus 로고    scopus 로고
    • Overexpression of phospholipase C-γ1 in rat 3Y1 fibroblast cells leads to malignant transformation
    • Chang, J. S., Noh, D. Y., Park, I. A., Kim, M. J., Song, H., Ryu, S. H., and Suh, P.-G. (1997) Overexpression of phospholipase C-γ1 in rat 3Y1 fibroblast cells leads to malignant transformation. Cancer Res. 57, 5465-5468
    • (1997) Cancer Res. , vol.57 , pp. 5465-5468
    • Chang, J.S.1    Noh, D.Y.2    Park, I.A.3    Kim, M.J.4    Song, H.5    Ryu, S.H.6    Suh, P.-G.7
  • 24
    • 0027527545 scopus 로고
    • Selectivity of ceramide-mediated biology. Lack of activity of erythro-dihydroceramide
    • Bielawska, A., Crane, H. M., Loitta, D., Obeid, L. M., and Hannun, Y. H. (1993) Selectivity of ceramide-mediated biology. Lack of activity of erythro-dihydroceramide. J. Biol. Chem. 268, 26226-26232
    • (1993) J. Biol. Chem. , vol.268 , pp. 26226-26232
    • Bielawska, A.1    Crane, H.M.2    Loitta, D.3    Obeid, L.M.4    Hannun, Y.H.5
  • 25
    • 0023805038 scopus 로고
    • Monoclonal antibodies to three phospholipase C isozymes from bovine brain
    • Suh, P.-G., Ryu, S. H., Choi, W. C., Lee, K.-Y., and Rhee, S. G. (1988) Monoclonal antibodies to three phospholipase C isozymes from bovine brain. J. Biol. Chem. 263, 14497-14504
    • (1988) J. Biol. Chem. , vol.263 , pp. 14497-14504
    • Suh, P.-G.1    Ryu, S.H.2    Choi, W.C.3    Lee, K.-Y.4    Rhee, S.G.5
  • 26
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, New York
    • Harlow, E., and Lane, D. (1988) Antibodies: A Laboratory Manual, pp. 53-119, Cold Spring Harbor Laboratory, Cold Spring Harbor, New York
    • (1988) Antibodies: A Laboratory Manual , pp. 53-119
    • Harlow, E.1    Lane, D.2
  • 29
    • 0026437690 scopus 로고
    • Expression, characterization and purification of soluble G-protein beta gamma dimers composed of defined subunits in baculovirus-infected insect cells
    • Dietrich, A., Meister, M., Spicher, K., Schultz, G., Camps, M., and Gierschik, P. (1992) Expression, characterization and purification of soluble G-protein beta gamma dimers composed of defined subunits in baculovirus-infected insect cells. FEBS Lett. 313, 220-224
    • (1992) FEBS Lett. , vol.313 , pp. 220-224
    • Dietrich, A.1    Meister, M.2    Spicher, K.3    Schultz, G.4    Camps, M.5    Gierschik, P.6
  • 31
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K., and Pease, L. R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene (Amst.) 77, 51-59
    • (1989) Gene (Amst.) , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 32
    • 0032566717 scopus 로고    scopus 로고
    • A functional role for mitochondrial protein kinase Cα in Bcl-2 phosphorylation and suppression of apoptosis
    • Ruvolo, P. P., Deng, X., Carr, B. K., and May, W. S. (1998) A functional role for mitochondrial protein kinase Cα in Bcl-2 phosphorylation and suppression of apoptosis. J. Biol. Chem. 273, 25436-25442
    • (1998) J. Biol. Chem. , vol.273 , pp. 25436-25442
    • Ruvolo, P.P.1    Deng, X.2    Carr, B.K.3    May, W.S.4
  • 33
    • 0030892234 scopus 로고    scopus 로고
    • Apoptosis by death factor
    • Nagata, S. (1997) Apoptosis by death factor. Cell 88, 355-365
    • (1997) Cell , vol.88 , pp. 355-365
    • Nagata, S.1
  • 34
    • 0031036872 scopus 로고    scopus 로고
    • Prevention of apoptosis by Bcl-2: Release of cytochrome c from mitochondria blocked
    • Yang, J., Liu, X., Bhalla, K., Kim, C. N., Ibrado, A. M., Cai, J., Peng, T.-I., Jones, D. P., and Wang, X. (1997) Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked. Science 275, 1129-1132
    • (1997) Science , vol.275 , pp. 1129-1132
    • Yang, J.1    Liu, X.2    Bhalla, K.3    Kim, C.N.4    Ibrado, A.M.5    Cai, J.6    Peng, T.-I.7    Jones, D.P.8    Wang, X.9
  • 36
    • 0031587921 scopus 로고    scopus 로고
    • Cloning of a SH3 domain-containing proline-rich protein, p85SPR, and its localization in focal adhesion
    • Oh, W. K., Yoo, J. C., Jo, D., Song, Y. H., Kim, M. G., Park, D. (1997) Cloning of a SH3 domain-containing proline-rich protein, p85SPR, and its localization in focal adhesion. Biochem. Biophys. Res. Commun. 235, 794-798
    • (1997) Biochem. Biophys. Res. Commun. , vol.235 , pp. 794-798
    • Oh, W.K.1    Yoo, J.C.2    Jo, D.3    Song, Y.H.4    Kim, M.G.5    Park, D.6
  • 37
    • 0028971813 scopus 로고
    • Phosphoinositide-specific phospholipase C and mitogenic signaling
    • Noh, D.-Y., Shin, S. H., and Rhee, S. G. (1995) Phosphoinositide-specific phospholipase C and mitogenic signaling. Biochim. Biophys. Acta 1242, 99-114
    • (1995) Biochim. Biophys. Acta , vol.1242 , pp. 99-114
    • Noh, D.-Y.1    Shin, S.H.2    Rhee, S.G.3
  • 38
    • 0025805394 scopus 로고
    • PDGF stimulation of inositol phospholipid hydrolysis requires PLC-γ1 phosphorylation on tyrosine residues 783 and 1254
    • Kim, H. K., Kim, J. W., Zilberstein, A., Margolis, B., Kim, J. G., Schlessinger, J., and Rhee, S. G. (1991) PDGF stimulation of inositol phospholipid hydrolysis requires PLC-γ1 phosphorylation on tyrosine residues 783 and 1254. Cell 65, 435-441
    • (1991) Cell , vol.65 , pp. 435-441
    • Kim, H.K.1    Kim, J.W.2    Zilberstein, A.3    Margolis, B.4    Kim, J.G.5    Schlessinger, J.6    Rhee, S.G.7
  • 39
    • 0032549670 scopus 로고    scopus 로고
    • Caspase-dependent cleavage of signaling proteins during apoptosis. A turn-off mechanism for anti-apoptotic signals
    • Widmann, C., Gibson, S., and Johnson, G. L. (1998) Caspase-dependent cleavage of signaling proteins during apoptosis. A turn-off mechanism for anti-apoptotic signals. J. Biol. Chem. 273, 7141-7147
    • (1998) J. Biol. Chem. , vol.273 , pp. 7141-7147
    • Widmann, C.1    Gibson, S.2    Johnson, G.L.3
  • 40
    • 0030613770 scopus 로고    scopus 로고
    • Phosphorylation of IkB-α inhibits its cleavage by caspase CPP32 in vitro
    • Barkett, M., Xue, D., Horvitz, H. R., and Gilmore, T. D. (1997) Phosphorylation of IkB-α inhibits its cleavage by caspase CPP32 in vitro. J. Biol. Chem. 272, 29419-29422
    • (1997) J. Biol. Chem. , vol.272 , pp. 29419-29422
    • Barkett, M.1    Xue, D.2    Horvitz, H.R.3    Gilmore, T.D.4
  • 41
    • 0028263973 scopus 로고
    • Epidermal growth factor-induced activation and translocation of phospholipase C-γ1 to the cytoskeleton in rat hepatocytes
    • Yang, L. J., Rhee, S. G., and Williamson, J. R. (1994) Epidermal growth factor-induced activation and translocation of phospholipase C-γ1 to the cytoskeleton in rat hepatocytes. J. Biol. Chem. 269, 7156-7162
    • (1994) J. Biol. Chem. , vol.269 , pp. 7156-7162
    • Yang, L.J.1    Rhee, S.G.2    Williamson, J.R.3
  • 42
    • 0032080004 scopus 로고    scopus 로고
    • Different subcellular distribution of caspase-3 and caspase-7 following Fas-induced apoptosis in mouse liver
    • Chandler, J. M., Cohen, G. M., MacFarlane, M. (1998) Different subcellular distribution of caspase-3 and caspase-7 following Fas-induced apoptosis in mouse liver. J. Biol. Chem. 273, 10815-10818
    • (1998) J. Biol. Chem. , vol.273 , pp. 10815-10818
    • Chandler, J.M.1    Cohen, G.M.2    MacFarlane, M.3
  • 43
    • 0027959158 scopus 로고
    • Limited proteolysis of phospholipase C-g1 indicates stable association of X and Y domains with enhanced catalytic activity
    • Fernald, A. W., Jones, G. A., and Carpenter, G. (1994) Limited proteolysis of phospholipase C-g1 indicates stable association of X and Y domains with enhanced catalytic activity. Biochem. J. 302, 503-509
    • (1994) Biochem. J. , vol.302 , pp. 503-509
    • Fernald, A.W.1    Jones, G.A.2    Carpenter, G.3
  • 44
    • 0030702123 scopus 로고    scopus 로고
    • Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
    • Datta, S. R., Dudek, H., Tao, X., Masters, S., Fu, H., Gotoh, Y., and Greenberg, M. E. (1997) Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell 91, 231-241
    • (1997) Cell , vol.91 , pp. 231-241
    • Datta, S.R.1    Dudek, H.2    Tao, X.3    Masters, S.4    Fu, H.5    Gotoh, Y.6    Greenberg, M.E.7


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