메뉴 건너뛰기




Volumn 19, Issue 10, 2000, Pages 2237-2246

Protein phosphatase 1α is a Ras-activated Bad phosphatase that regulates interleukin-2 deprivation-induced apoptosis

Author keywords

Apoptosis; Bad; Interleukin 2; Protein phosphatase PP1 ; Ras

Indexed keywords

GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; INTERLEUKIN 2; OKADAIC ACID; PHOSPHOPROTEIN PHOSPHATASE; PROTEIN BAD; RAS PROTEIN; SERINE; BAD PROTEIN, MOUSE; CARRIER PROTEIN;

EID: 0342657806     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/19.10.2237     Document Type: Article
Times cited : (123)

References (58)
  • 1
    • 0032575688 scopus 로고    scopus 로고
    • The Bcl-2 protein family: Arbiters of cell survival
    • Adams, J.M. and Cory, S. (1998) The Bcl-2 protein family: arbiters of cell survival. Science, 281, 1322-1326.
    • (1998) Science , vol.281 , pp. 1322-1326
    • Adams, J.M.1    Cory, S.2
  • 2
    • 0027458292 scopus 로고
    • Regulation of cell cycle progression and nuclear affinity of the Rb protein by protein phosphatases
    • Alberts, A.S., Thorburn, A.M., Shenolikar, S., Mumby, M.C. and Feramisco, J.R. (1993) Regulation of cell cycle progression and nuclear affinity of the Rb protein by protein phosphatases. Proc. Natl Acad. Sci. USA. 90, 388-392.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 388-392
    • Alberts, A.S.1    Thorburn, A.M.2    Shenolikar, S.3    Mumby, M.C.4    Feramisco, J.R.5
  • 3
    • 0025011050 scopus 로고
    • One of the protein phosphatase 1 isoenzymes in Drosophila is essential for mitosis
    • Axton, J.M., Dombradi, V., Cohen, P.T. and Glover, D.M. (1990) One of the protein phosphatase 1 isoenzymes in Drosophila is essential for mitosis. Cell, 63, 33-46.
    • (1990) Cell , vol.63 , pp. 33-46
    • Axton, J.M.1    Dombradi, V.2    Cohen, P.T.3    Glover, D.M.4
  • 4
    • 0345517990 scopus 로고    scopus 로고
    • Reduction of H-Ras induced cellular transformation by elevated expression of protein phosphatase type 2A
    • Baharians, Z. and Schönthal, A.H. (1999) Reduction of H-Ras induced cellular transformation by elevated expression of protein phosphatase type 2A. Mol. Carcinog., 24, 246-254.
    • (1999) Mol. Carcinog. , vol.24 , pp. 246-254
    • Baharians, Z.1    Schönthal, A.H.2
  • 7
    • 0032698075 scopus 로고    scopus 로고
    • Cell survival promoted by the Ras-MAPK signaling pathway by transcription-dependent and -independent mechanisms
    • Bonni, A., Brunet, A., Liu, M.Z. and Greenberg, M.E. (1999) Cell survival promoted by the Ras-MAPK signaling pathway by transcription-dependent and -independent mechanisms. Science, 286, 1358-1362.
    • (1999) Science , vol.286 , pp. 1358-1362
    • Bonni, A.1    Brunet, A.2    Liu, M.Z.3    Greenberg, M.E.4
  • 8
    • 0031918223 scopus 로고    scopus 로고
    • Bcl-2 family: Regulators of cell death
    • Chao, D.T. and Korsmeyer, S.J. (1998) Bcl-2 family: regulators of cell death. Annu. Rev. Immunol. 16. 395-410.
    • (1998) Annu. Rev. Immunol. , vol.16 , pp. 395-410
    • Chao, D.T.1    Korsmeyer, S.J.2
  • 9
    • 0034695599 scopus 로고    scopus 로고
    • Serine/threonine protein phosphatase type 1γ is required for the completion of cytokinesis in human A549 lung carcinoma cells
    • Cheng, A., Dean, N.M. and Honkanen, R.E. (2000) Serine/threonine protein phosphatase type 1γ is required for the completion of cytokinesis in human A549 lung carcinoma cells. J. Biol. Chem., 275, 1846-1854.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1846-1854
    • Cheng, A.1    Dean, N.M.2    Honkanen, R.E.3
  • 10
  • 11
    • 0024361302 scopus 로고
    • An improved procedure for identifying and quantitating protein phosphatases in mammalian tissues
    • Cohen, P., Klumpp, S. and Schelling, D.L. (1989) An improved procedure for identifying and quantitating protein phosphatases in mammalian tissues. FEBS Lett., 250, 596-600.
    • (1989) FEBS Lett. , vol.250 , pp. 596-600
    • Cohen, P.1    Klumpp, S.2    Schelling, D.L.3
  • 12
    • 0025181418 scopus 로고
    • Okadaic acid: A new probe for the study of cellular regulation
    • Cohen, P., Holmes, C.F. and Tsukitani, Y. (1990) Okadaic acid: a new probe for the study of cellular regulation. Trends Biochem. Sci., 15, 98-102.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 98-102
    • Cohen, P.1    Holmes, C.F.2    Tsukitani, Y.3
  • 13
    • 0028915454 scopus 로고
    • Regulation of lymphocyte survival by the Bcl-2 gene family
    • Cory, S. (1995) Regulation of lymphocyte survival by the Bcl-2 gene family. Annu. Rev. Immunol. 13, 513-543.
    • (1995) Annu. Rev. Immunol. , vol.13 , pp. 513-543
    • Cory, S.1
  • 14
    • 0033537849 scopus 로고    scopus 로고
    • Dissociation of apoptosis from proliferation. PKB activation and Bad phosphorylation in IL-3-mediated P13 kinase signaling
    • Craddock, B.L., Orchiston, E.A., Hinton, H. and Welham, M.J. (1999) Dissociation of apoptosis from proliferation. PKB activation and Bad phosphorylation in IL-3-mediated P13 kinase signaling. J. Biol. Chem., 274, 10633-10640.
    • (1999) J. Biol. Chem. , vol.274 , pp. 10633-10640
    • Craddock, B.L.1    Orchiston, E.A.2    Hinton, H.3    Welham, M.J.4
  • 15
    • 0030702123 scopus 로고    scopus 로고
    • Akt phosphorylation of Bad couples survival signals to the cell-intrinsic death machinery
    • Datta, S.R., Dukek, 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    Dukek, H.2    Tao, X.3    Masters, S.4    Gotoh, Y.5    Greenberg, M.E.6
  • 16
    • 1842333237 scopus 로고    scopus 로고
    • Interleukin-3-induced phosphorylation of Bad through the protein kinase Akt
    • del Peso, L., Garcia, M.G., Page, C., Herrera, R. and Nuñez, G. (1997) Interleukin-3-induced phosphorylation of Bad through the protein kinase Akt. Science, 278, 687-689.
    • (1997) Science , vol.278 , pp. 687-689
    • Del Peso, L.1    Garcia, M.G.2    Page, C.3    Herrera, R.4    Nuñez, G.5
  • 17
    • 0343457526 scopus 로고    scopus 로고
    • Reversible phosphorylation of Bcl-2 following IL-3 or Bryoslatin 1 is mediated by direct interaction with protein phosphatase 2A
    • Deng, X., Ito, T., Carr, B., Mumby, M. and Stratford, M.J. (1998) Reversible phosphorylation of Bcl-2 following IL-3 or Bryoslatin 1 is mediated by direct interaction with protein phosphatase 2A. J. Biol. Chem., 273, 34157-34163.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34157-34163
    • Deng, X.1    Ito, T.2    Carr, B.3    Mumby, M.4    Stratford, M.J.5
  • 20
    • 0030219389 scopus 로고    scopus 로고
    • More on targeting with protein phosphorylation: Conferring specificity by location
    • Faux, M.C. and Scott, J.D. (1996) More on targeting with protein phosphorylation: conferring specificity by location. Trends Biochem. Sci., 21, 312-315.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 312-315
    • Faux, M.C.1    Scott, J.D.2
  • 21
    • 0030924806 scopus 로고    scopus 로고
    • Differential inhibition and posttranslational modification of protein phosphatase 1 and 2A in MCF7 cells treated with calyculin, okadaic acid and tautomycin
    • Favre, B., Turowski, P. and Hemmings, B.A. (1997) Differential inhibition and posttranslational modification of protein phosphatase 1 and 2A in MCF7 cells treated with calyculin, okadaic acid and tautomycin. J. Biol. Chem., 272, 13856-13863.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13856-13863
    • Favre, B.1    Turowski, P.2    Hemmings, B.A.3
  • 22
    • 0032504967 scopus 로고    scopus 로고
    • The Bcl-2 gene is differentially regulated by IL-2 and IL-4: Role of the transcription factor NF-AT
    • Gómez, J., Martínez-A.C., González, A., García, A. and Rebollo, A. (1998) The Bcl-2 gene is differentially regulated by IL-2 and IL-4: role of the transcription factor NF-AT. Oncogene, 17, 1235-1243.
    • (1998) Oncogene , vol.17 , pp. 1235-1243
    • Gómez, J.1    González, A.2    García, A.3    Rebollo, A.4
  • 24
    • 0031017382 scopus 로고    scopus 로고
    • The y protein of herpes simplex virus complexes with PP1α to dephosphorylate the a subunit of eukaryotic TIF2 and preclude the shut off of protein synthesis by double strand RNA-activated protein kinase
    • He, B., Gross, M. and Roizman, B. (1997) The y protein of herpes simplex virus complexes with PP1α to dephosphorylate the a subunit of eukaryotic TIF2 and preclude the shut off of protein synthesis by double strand RNA-activated protein kinase. Proc. Natl Acad. Sci. USA, 94, 843-848.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 843-848
    • He, B.1    Gross, M.2    Roizman, B.3
  • 25
    • 2142721829 scopus 로고    scopus 로고
    • Interference of Bad-induced apoptosis in mammalian cells by 14-3-3 isoforms and P11
    • Hsu, S.Y., Kaipai, L., Zhu, L. and Hsueh, A.J. (1997) Interference of Bad-induced apoptosis in mammalian cells by 14-3-3 isoforms and P11. Mol. Endocrinol., 11, 1858-1867.
    • (1997) Mol. Endocrinol. , vol.11 , pp. 1858-1867
    • Hsu, S.Y.1    Kaipai, L.2    Zhu, L.3    Hsueh, A.J.4
  • 26
    • 0027277098 scopus 로고
    • On target with new mechanism for the regulation of protein phosphorylation
    • Hubbard, M.J. and Cohen, P. (1993) On target with new mechanism for the regulation of protein phosphorylation. Trends Biochem. Sci., 18, 172-177.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 172-177
    • Hubbard, M.J.1    Cohen, P.2
  • 27
    • 0020540151 scopus 로고
    • The protein phosphatases involved in cellular regulation. Classification and substrate specificities
    • Ingebritsen, T.S. and Cohen, P. (1983) The protein phosphatases involved in cellular regulation. Classification and substrate specificities. Eur. J. Biochem., 132, 255-261.
    • (1983) Eur. J. Biochem. , vol.132 , pp. 255-261
    • Ingebritsen, T.S.1    Cohen, P.2
  • 28
    • 0031148667 scopus 로고    scopus 로고
    • Apoptosis: Bcl-2-related proteins get connected
    • Jacobson, M.D. (1997) Apoptosis: Bcl-2-related proteins get connected. Curr. Biol., 7, 277-281.
    • (1997) Curr. Biol. , vol.7 , pp. 277-281
    • Jacobson, M.D.1
  • 29
    • 0030695837 scopus 로고    scopus 로고
    • Bad is a BH3-containing protein that forms an inactivating dimer with Bcl-x
    • Kelekar, A., Chang, B.S., Harlan, J.E., Fesik, S.S. and Thompson, C.B. (1997) Bad is a BH3-containing protein that forms an inactivating dimer with Bcl-x. Mol. Cell. Biol. 17, 7040-7046.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 7040-7046
    • Kelekar, A.1    Chang, B.S.2    Harlan, J.E.3    Fesik, S.S.4    Thompson, C.B.5
  • 30
    • 0024996931 scopus 로고
    • Distinct essential roles of type 1 and 2A protein phosphatases in the control of the fission yeast cell division cycle
    • Kinoshita, N., Ohkura, H. and Yanagida, M. (1990) Distinct essential roles of type 1 and 2A protein phosphatases in the control of the fission yeast cell division cycle. Cell, 63, 405-415.
    • (1990) Cell , vol.63 , pp. 405-415
    • Kinoshita, N.1    Ohkura, H.2    Yanagida, M.3
  • 31
    • 0031017969 scopus 로고    scopus 로고
    • Separation of PP2A core enzyme and holoenzyme with monoclonal antibodies against the regulatory A subunit: Abundant expression of both forms in T cells
    • Kremmer, E., Ohst, K., Kiefer, J. and Walter, G. (1997) Separation of PP2A core enzyme and holoenzyme with monoclonal antibodies against the regulatory A subunit: abundant expression of both forms in T cells. Mol. Cell. Biol., 17, 1692-1701.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1692-1701
    • Kremmer, E.1    Ohst, K.2    Kiefer, J.3    Walter, G.4
  • 33
    • 0025908180 scopus 로고
    • Modulation of type I protein phosphatase by synthetic peptides corresponding to the carboxyl terminus
    • Martin, B.L., Shriner, C.L. and Brautigan, D.L. (1991) Modulation of type I protein phosphatase by synthetic peptides corresponding to the carboxyl terminus. FEBS Lett., 285, 6-10.
    • (1991) FEBS Lett. , vol.285 , pp. 6-10
    • Martin, B.L.1    Shriner, C.L.2    Brautigan, D.L.3
  • 34
    • 0027143725 scopus 로고
    • Protein serine/threonine phosphatases: Structure, regulation and functions in cell growth
    • Mumby, M.C. and Walter, G.W. (1993) Protein serine/threonine phosphatases: structure, regulation and functions in cell growth. Physiol. Rev., 73, 673-699.
    • (1993) Physiol. Rev. , vol.73 , pp. 673-699
    • Mumby, M.C.1    Walter, G.W.2
  • 35
    • 0027525536 scopus 로고
    • Targeting of Bcl-2 to the mitochondrial outer membrane by a COOH-terminal signal anchor sequence
    • Nguyen, M., Millar, D.G., Yong, V.W., Korsmeyer, S.J. and Shore, G.C. (1993) Targeting of Bcl-2 to the mitochondrial outer membrane by a COOH-terminal signal anchor sequence. J. Biol. Chem., 268, 25265-25268.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25265-25268
    • Nguyen, M.1    Millar, D.G.2    Yong, V.W.3    Korsmeyer, S.J.4    Shore, G.C.5
  • 36
    • 0030707613 scopus 로고    scopus 로고
    • Dimerization properties of human Bad
    • Ottilie, S. et al. (1997) Dimerization properties of human Bad. J. Biol. Chem., 272, 30866-30872.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30866-30872
    • Ottilie, S.1
  • 37
    • 0033516674 scopus 로고    scopus 로고
    • TNF induces phosphorylation and translocation of Bad through a P13 kinase-dependent pathway
    • Pastorino, J.G., Tafani, M. and Farber, J.L. (1999) TNF induces phosphorylation and translocation of Bad through a P13 kinase-dependent pathway. J. Biol. Chem., 274, 19411-19416.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19411-19416
    • Pastorino, J.G.1    Tafani, M.2    Farber, J.L.3
  • 38
    • 0027521474 scopus 로고
    • High affinity and intermediate affinity forms of the human IL-2 receptor expressed in an IL-9-dependent murine T cell line deliver proliferative signals via differences in their transduction pathways
    • Pitton, C., Rebollo, A., Van Snick, J., Theze, J. and Garcia, A. (1993) High affinity and intermediate affinity forms of the human IL-2 receptor expressed in an IL-9-dependent murine T cell line deliver proliferative signals via differences in their transduction pathways. Cytokine, 5, 362-371.
    • (1993) Cytokine , vol.5 , pp. 362-371
    • Pitton, C.1    Rebollo, A.2    Van Snick, J.3    Theze, J.4    Garcia, A.5
  • 39
    • 0032818585 scopus 로고    scopus 로고
    • Ras mutation, irrespective of cell type and p53 status, determines a cell's destiny to undergo apoptosis by okadaic acid, an inhibitor of protein phosphatase 1 and 2A
    • Rajesh, D., Schell, K. and Verma, A.K. (1999) Ras mutation, irrespective of cell type and p53 status, determines a cell's destiny to undergo apoptosis by okadaic acid, an inhibitor of protein phosphatase 1 and 2A. Mol. Pharmacol., 56, 515-525.
    • (1999) Mol. Pharmacol. , vol.56 , pp. 515-525
    • Rajesh, D.1    Schell, K.2    Verma, A.K.3
  • 40
    • 0030979773 scopus 로고    scopus 로고
    • Double identity for proteins of the Bcl-2 family
    • Reed, J.C. (1997) Double identity for proteins of the Bcl-2 family. Nature, 387, 773-776.
    • (1997) Nature , vol.387 , pp. 773-776
    • Reed, J.C.1
  • 41
    • 0025641204 scopus 로고
    • Identification of members of the PP1 gene family in the rat and enhanced expression of PP1α gene in rat hepatocellular carcinoma
    • Sasaki, K., Shima, H., Kitagawa, Y., Irino, S., Sugimura, T. and Nagao, M. (1990) Identification of members of the PP1 gene family in the rat and enhanced expression of PP1α gene in rat hepatocellular carcinoma. Jpn. J. Cancer Res., 81, 1272-1280.
    • (1990) Jpn. J. Cancer Res. , vol.81 , pp. 1272-1280
    • Sasaki, K.1    Shima, H.2    Kitagawa, Y.3    Irino, S.4    Sugimura, T.5    Nagao, M.6
  • 42
    • 0032560514 scopus 로고    scopus 로고
    • Dissociation of cytokine-induced phosphorylation of Bad and activation of PKB/Akt: Involvement of MEK upstream of Bad phosphorylation
    • Scheid, M.P. and Duronio, V. (1998) Dissociation of cytokine-induced phosphorylation of Bad and activation of PKB/Akt: involvement of MEK upstream of Bad phosphorylation. Proc. Natl Acad. Sci. USA, 95, 7439-7444.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 7439-7444
    • Scheid, M.P.1    Duronio, V.2
  • 43
    • 0032747134 scopus 로고    scopus 로고
    • Regulation of Bad phosphorylation and association with Bcl-x by the MAPK/Erk kinase
    • Scheid, M.P., Schubert, K.M. and Duronio, V. (1999) Regulation of Bad phosphorylation and association with Bcl-x by the MAPK/Erk kinase. J. Biol. Chem., 274, 31108-31113.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31108-31113
    • Scheid, M.P.1    Schubert, K.M.2    Duronio, V.3
  • 45
    • 0028170809 scopus 로고
    • Protein serine/threonine phosphatases, new avenues for cell regulation
    • Shenolikar, S. (1994) Protein serine/threonine phosphatases, new avenues for cell regulation. Annu. Rev. Cell. Biol., 10, 55-86.
    • (1994) Annu. Rev. Cell. Biol. , vol.10 , pp. 55-86
    • Shenolikar, S.1
  • 47
    • 0033214325 scopus 로고    scopus 로고
    • A PP2A regulatory subunit positively regulates Ras-mediated signaling during C.elegans vulval induction
    • Sieburth, D.S., Sundaram, M., Howard, R.M. and Han, M. (1999) A PP2A regulatory subunit positively regulates Ras-mediated signaling during C.elegans vulval induction. Genes Dev., 13, 2562-2569.
    • (1999) Genes Dev. , vol.13 , pp. 2562-2569
    • Sieburth, D.S.1    Sundaram, M.2    Howard, R.M.3    Han, M.4
  • 48
    • 0030769625 scopus 로고    scopus 로고
    • Protein phosphatase 2A is a critical regulator of PKC ζ signaling targeted by SV40 small t to promote cell growth and NF-κB activation
    • Sontag, E., Sontag, J.M. and García, A. (1997) Protein phosphatase 2A is a critical regulator of PKC ζ signaling targeted by SV40 small t to promote cell growth and NF-κB activation. EMBO J., 16, 5662-5671.
    • (1997) EMBO J. , vol.16 , pp. 5662-5671
    • Sontag, E.1    Sontag, J.M.2    García, A.3
  • 49
    • 0033584231 scopus 로고    scopus 로고
    • Bcl-2-mediated drug resistance: Inhibition of apoptosis by blocking nuclear factor of activated T cells (NFAT)-induced fas ligand transcription
    • Srivastaba, R.K., Sasaki, C.Y., Hardwick, J.M. and Logo, D.L. (1999) Bcl-2-mediated drug resistance: inhibition of apoptosis by blocking nuclear factor of activated T cells (NFAT)-induced Fas ligand transcription. J. Exp. Med., 190, 253-266.
    • (1999) J. Exp. Med. , vol.190 , pp. 253-266
    • Srivastaba, R.K.1    Sasaki, C.Y.2    Hardwick, J.M.3    Logo, D.L.4
  • 50
    • 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
  • 51
    • 0028978217 scopus 로고
    • Activation of NF-κB by phosphatase inhibitors involves the phosphorylation of 1KB at phosphatase 2A sensitive sites
    • Sun, S.C., Maggirwar, S.B. and Harhaj, E. (1995) Activation of NF-κB by phosphatase inhibitors involves the phosphorylation of 1KB at phosphatase 2A sensitive sites. J. Biol. Chem., 270, 18347-18351.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18347-18351
    • Sun, S.C.1    Maggirwar, S.B.2    Harhaj, E.3
  • 52
    • 0028094638 scopus 로고
    • Tissue distribution of isoforms of type I PP1 in mouse tissues and its diabetic alterations
    • Takizawa, N., Mizuno, Y., Ito, Y. and Kikuchi, K. (1994) Tissue distribution of isoforms of type I PP1 in mouse tissues and its diabetic alterations. J. Biochem., 116, 411-415.
    • (1994) J. Biochem. , vol.116 , pp. 411-415
    • Takizawa, N.1    Mizuno, Y.2    Ito, Y.3    Kikuchi, K.4
  • 53
    • 0033537768 scopus 로고    scopus 로고
    • ++-induced apoptosis through calcineurin dephosphorylation of Bad
    • ++-induced apoptosis through calcineurin dephosphorylation of Bad. Science, 284, 339-343.
    • (1999) Science , vol.284 , pp. 339-343
    • Wang, H.G.1
  • 54
    • 0029129557 scopus 로고
    • Serine/threonine protein phosphatases
    • Wera, S. and Hemmings, B.A. (1995) Serine/threonine protein phosphatases. Biochem. J., 311, 17-29.
    • (1995) Biochem. J. , vol.311 , pp. 17-29
    • Wera, S.1    Hemmings, B.A.2
  • 55
    • 0028003818 scopus 로고
    • Phosphorylation of dis2 protein phosphatase at the C-terninal cdc2 consensus and its potential role in cell cycle regulation
    • Yamano, H., Ishii, K. and Yanagida, M. (1994) Phosphorylation of dis2 protein phosphatase at the C-terninal cdc2 consensus and its potential role in cell cycle regulation. EMBO J., 13, 5310-5318.
    • (1994) EMBO J. , vol.13 , pp. 5310-5318
    • Yamano, H.1    Ishii, K.2    Yanagida, M.3
  • 56
    • 0028809209 scopus 로고
    • Bad: A heterodimeric partner for Bcl-x and Bcl-2 displaces bax and promotes cell death
    • Yang, E., Zha, J., Jockel, J., Boise, L.H., Thompson, C.B. and Korsmeyer, S.J. (1995) Bad: a heterodimeric partner for Bcl-x and Bcl-2 displaces Bax and promotes cell death. Cell, 80, 285-291.
    • (1995) Cell , vol.80 , pp. 285-291
    • Yang, E.1    Zha, J.2    Jockel, J.3    Boise, L.H.4    Thompson, C.B.5    Korsmeyer, S.J.6
  • 57
    • 0030584088 scopus 로고    scopus 로고
    • Serine phosphorylation of death agonist Bad in response to survival factor results in binding to 14-3-3 not Bcl-x
    • Zha, J., Harada, H., Yang, E., Jocker, J. and Korsmeyer, S. (1996) Serine phosphorylation of death agonist Bad in response to survival factor results in binding to 14-3-3 not Bcl-x. Cell, 87, 619-628.
    • (1996) Cell , vol.87 , pp. 619-628
    • Zha, J.1    Harada, H.2    Yang, E.3    Jocker, J.4    Korsmeyer, S.5
  • 58
    • 0030827971 scopus 로고    scopus 로고
    • BH3 domain of Bad is required for heterodimerization with Bcl-x and pro-apoptotic activity
    • Zha, J., Harada, H., Osipov, K., Jockel, J., Waksman, G. and Korsmeyer, S.J. (1997) BH3 domain of Bad is required for heterodimerization with Bcl-x and pro-apoptotic activity. J. Biol. Chem., 272, 24101-24104.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24101-24104
    • Zha, J.1    Harada, H.2    Osipov, K.3    Jockel, J.4    Waksman, G.5    Korsmeyer, S.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.