메뉴 건너뛰기




Volumn 23, Issue 18, 2003, Pages 6350-6362

Protein phosphatase 2A dephosphorylation of phosphoserine 112 plays the gatekeeper role for BAD-mediated apoptosis

Author keywords

[No Author keywords available]

Indexed keywords

INTERLEUKIN 3; PHOSPHOPROTEIN PHOSPHATASE 2A; PHOSPHOSERINE; PROTEIN BAD; PROTEIN BCL 2; PROTEIN BCL XL; SERINE; THREONINE;

EID: 0043193866     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.23.18.6350-6362.2003     Document Type: Article
Times cited : (131)

References (45)
  • 1
    • 0035146929 scopus 로고    scopus 로고
    • Life-or-death decisions by the Bcl-2 protein family
    • Adams, J. M., and S. Cory. 2001. Life-or-death decisions by the Bcl-2 protein family. Trends Biochem. Sci. 26:61-66.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 61-66
    • Adams, J.M.1    Cory, S.2
  • 3
    • 0342657806 scopus 로고    scopus 로고
    • Protein phosphatase 1alpha is a Ras-activated Bad phosphatase that regulates interleukin-2 deprivation-induced apoptosis
    • Ayllon, V., A. C. Martinez, A. Garcia, X. Cayla, and A. Rebollo. 2000. Protein phosphatase 1alpha is a Ras-activated Bad phosphatase that regulates interleukin-2 deprivation-induced apoptosis. EMBO J. 19:2237-2246.
    • (2000) EMBO J. , vol.19 , pp. 2237-2246
    • Ayllon, V.1    Martinez, A.C.2    Garcia, A.3    Cayla, X.4    Rebollo, A.5
  • 4
    • 0034711239 scopus 로고    scopus 로고
    • Protein kinase C theta and epsilon promote T-cell survival by a Rsk-dependent phosphorylation and inactivation of BAD
    • Bertolotto, C., L. Maulon, N. Filippa, G. Baier, and P. Auberger. 2000. Protein kinase C theta and epsilon promote T-cell survival by a Rsk-dependent phosphorylation and inactivation of BAD. J. Biol. Chem. 275:37246-37250.
    • (2000) J. Biol. Chem. , vol.275 , pp. 37246-37250
    • Bertolotto, C.1    Maulon, L.2    Filippa, N.3    Baier, G.4    Auberger, P.5
  • 5
    • 0032698075 scopus 로고    scopus 로고
    • Cell survival promoted by the Ras-MAPK signaling pathway by transcription-dependent and -independent mechanisms
    • Bonni, A., A. Brunet, A. E. West, S. R. Datta, M. A. Takasu, and M. E. Greenberg. 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    West, A.E.3    Datta, S.R.4    Takasu, M.A.5    Greenberg, M.E.6
  • 6
    • 0035283087 scopus 로고    scopus 로고
    • Protein phosphatase 2A activates the proapoptotic function of BAD in interleukin-3-dependent lymphoid cells by a mechanism requiring 14-3-3 dissociation
    • Chiang, C. W., G. Harris, C. Ellig, S. C. Masters, R. Subramanian, S. Shenolikar, B. E. Wadzinski, and E. Yang. 2001. Protein phosphatase 2A activates the proapoptotic function of BAD in interleukin-3-dependent lymphoid cells by a mechanism requiring 14-3-3 dissociation. Blood 97:1289-1297.
    • (2001) Blood , vol.97 , pp. 1289-1297
    • Chiang, C.W.1    Harris, G.2    Ellig, C.3    Masters, S.C.4    Subramanian, R.5    Shenolikar, S.6    Wadzinski, B.E.7    Yang, E.8
  • 8
    • 0030702123 scopus 로고    scopus 로고
    • Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
    • Datta, S. R., H. Dudek, X. Tao, S. Masters, H. Fu, Y. Gotoh, and M. E. Greenberg. 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
  • 9
    • 0033635235 scopus 로고    scopus 로고
    • 14-3-3 Proteins and survival kinases cooperate to inactivate BAD by BH3 domain phosphorylation
    • Datta, S. R., A. Katsov, L. Hu, A. Petros, S. W. Fesik, M. B. Yaffe, and M. E. Greenberg. 2000. 14-3-3 proteins and survival kinases cooperate to inactivate BAD by BH3 domain phosphorylation. Mol. Cell 6:41-51.
    • (2000) Mol. Cell , vol.6 , pp. 41-51
    • Datta, S.R.1    Katsov, A.2    Hu, L.3    Petros, A.4    Fesik, S.W.5    Yaffe, M.B.6    Greenberg, M.E.7
  • 13
    • 0030698062 scopus 로고    scopus 로고
    • 14-3-3 Is phosphorylated by case in kinase I on residue 233. Phosphorylation at this site in vivo regulates Raf/14-3-3 interaction
    • Dubois, T., C. Rommel, S. Howell, U. Steinhussen, Y. Soneji, N. Morrice, K. Moelling, and A. Aitken. 1997. 14-3-3 is phosphorylated by case in kinase I on residue 233. Phosphorylation at this site in vivo regulates Raf/14-3-3 interaction. J. Biol. Chem. 272:28882-28888.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28882-28888
    • Dubois, T.1    Rommel, C.2    Howell, S.3    Steinhussen, U.4    Soneji, Y.5    Morrice, N.6    Moelling, K.7    Aitken, A.8
  • 14
    • 0035859956 scopus 로고    scopus 로고
    • p70S6 kinase signals cell survival as well as growth, inactivating the proapoptotic molecule BAD
    • Harada, H., J. S. Andersen, M. Mann, N. Terada, and S. J. Korsmeyer. 2001. p70S6 kinase signals cell survival as well as growth, inactivating the proapoptotic molecule BAD. Proc. Natl. Acad. Sci. USA 98:9666-9670.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9666-9670
    • Harada, H.1    Andersen, J.S.2    Mann, M.3    Terada, N.4    Korsmeyer, S.J.5
  • 16
    • 0032563347 scopus 로고    scopus 로고
    • Purification of protein phosphatase 4 catalytic subunit: Inhibition by the antitumour drug fostriecin and other tumour suppressors and promoters
    • Hastie, C. J., and P. T. Cohen. 1998. Purification of protein phosphatase 4 catalytic subunit: inhibition by the antitumour drug fostriecin and other tumour suppressors and promoters, FEBS Lett. 431:357-361.
    • (1998) FEBS Lett. , vol.431 , pp. 357-361
    • Hastie, C.J.1    Cohen, P.T.2
  • 17
    • 0033635733 scopus 로고    scopus 로고
    • BH3-Only proteins-essential initiators of apoptotic cell death
    • Huang, D. C., and A. Strasser. 2000. BH3-Only proteins-essential initiators of apoptotic cell death. Cell 103:839-842.
    • (2000) Cell , vol.103 , pp. 839-842
    • Huang, D.C.1    Strasser, A.2
  • 18
    • 0035252894 scopus 로고    scopus 로고
    • Protein phosphatase 2A: A highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling
    • Janssens, V., and J. Goris. 2001. Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling. Biochem. J. 353:417-439.
    • (2001) Biochem. J. , vol.353 , pp. 417-439
    • Janssens, V.1    Goris, J.2
  • 19
    • 0036282745 scopus 로고    scopus 로고
    • Cdc2 phosphorylation of BAD links the cell cycle to the cell death machinery
    • Konishi, Y., M. Lehtinen, N. Donovan, and A. Bonni. 2002. Cdc2 phosphorylation of BAD links the cell cycle to the cell death machinery. Mol. Cell 9:1005-1016.
    • (2002) Mol. Cell , vol.9 , pp. 1005-1016
    • Konishi, Y.1    Lehtinen, M.2    Donovan, N.3    Bonni, A.4
  • 20
    • 0034661857 scopus 로고    scopus 로고
    • Regulation of BAD by cAMP-dependent protein kinase is mediated via phosphorylation of a novel site, Ser155
    • Lizcano, J. M., N. Morrice, and P. Cohen. 2000. Regulation of BAD by cAMP-dependent protein kinase is mediated via phosphorylation of a novel site, Ser155. Biochem. J. 349:547-557.
    • (2000) Biochem. J. , vol.349 , pp. 547-557
    • Lizcano, J.M.1    Morrice, N.2    Cohen, P.3
  • 21
    • 0033965412 scopus 로고    scopus 로고
    • Role of the BH3 (Bcl-2 homology 3) domain in the regulation of apoptosis and Bcl-2-related proteins
    • Lutz, R. J. 2000. Role of the BH3 (Bcl-2 homology 3) domain in the regulation of apoptosis and Bcl-2-related proteins. Biochem. Soc. Trans. 28:51-56.
    • (2000) Biochem. Soc. Trans. , vol.28 , pp. 51-56
    • Lutz, R.J.1
  • 22
    • 0038021272 scopus 로고    scopus 로고
    • Control of apoptosis in the immune system: Bcl-2, BH3-only proteins and more
    • Marsden, V. S., and A. Strasser. 2003. Control of apoptosis in the immune system: Bcl-2, BH3-only proteins and more. Annu. Rev. Immunol. Rev. 21:71-105.
    • (2003) Annu. Rev. Immunol. Rev. , vol.21 , pp. 71-105
    • Marsden, V.S.1    Strasser, A.2
  • 23
    • 0035939812 scopus 로고    scopus 로고
    • The growth-promoting activity of the Bad protein in chicken embryo fibroblasts requires binding to protein 14-3-3
    • Maslyar, D. J., M. Aoki, and P. K. Vogt. 2001. The growth-promoting activity of the Bad protein in chicken embryo fibroblasts requires binding to protein 14-3-3. Oncogene 20:5087-5092.
    • (2001) Oncogene , vol.20 , pp. 5087-5092
    • Maslyar, D.J.1    Aoki, M.2    Vogt, P.K.3
  • 25
    • 0035206813 scopus 로고    scopus 로고
    • 14-3-3 Inhibits Bad-induced cell death through interaction with serine-136
    • Masters, S. C., H. Yang, S. R. Datta, M. E. Greenberg, and H. Fu. 2001. 14-3-3 inhibits Bad-induced cell death through interaction with serine-136. Mol. Pharmacol. 60:1325-1331.
    • (2001) Mol. Pharmacol. , vol.60 , pp. 1325-1331
    • Masters, S.C.1    Yang, H.2    Datta, S.R.3    Greenberg, M.E.4    Fu, H.5
  • 26
    • 0029871708 scopus 로고    scopus 로고
    • Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine
    • Muslin, A. J., J. W. Tanner, P. M. Allen, and A. S. Shaw. 1996. Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell 84:889-897.
    • (1996) Cell , vol.84 , pp. 889-897
    • Muslin, A.J.1    Tanner, J.W.2    Allen, P.M.3    Shaw, A.S.4
  • 28
    • 0033575320 scopus 로고    scopus 로고
    • Ceramide induces Bcl2 dephosphorylation via a mechanism involving mitochondrial PP2A
    • Ruvolo, P. P., X. Deng, T. Ito, B. K. Carr, and W. S. May. 1999. Ceramide induces Bcl2 dephosphorylation via a mechanism involving mitochondrial PP2A. J. Biol. Chem. 274:20296-20300.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20296-20300
    • Ruvolo, P.P.1    Deng, X.2    Ito, T.3    Carr, B.K.4    May, W.S.5
  • 29
    • 0035073292 scopus 로고    scopus 로고
    • Phosphorylation of Bcl2 and regulation of apoptosis
    • Ruvolo, P. P., X. Deng, and W. S. May. 2001. Phosphorylation of Bcl2 and regulation of apoptosis. Leukemia 15:515-522.
    • (2001) Leukemia , vol.15 , pp. 515-522
    • Ruvolo, P.P.1    Deng, X.2    May, W.S.3
  • 30
    • 0034662158 scopus 로고    scopus 로고
    • Versatility of BCR/ABL-expressing leukemic cells in circumventing proapoptotic BAD effects
    • Salomoni, P., F. Condorelli, S. M. Sweeney, and B. Calabretta. 2000. Versatility of BCR/ABL-expressing leukemic cells in circumventing proapoptotic BAD effects. Blood 96:676-684.
    • (2000) Blood , vol.96 , pp. 676-684
    • Salomoni, P.1    Condorelli, F.2    Sweeney, S.M.3    Calabretta, B.4
  • 32
  • 33
    • 0034682812 scopus 로고    scopus 로고
    • BAD Ser-155 phosphorylation regulates BAD/Bcl-XL interaction and cell survival
    • Tan, Y., M. R. Demeter, H. Ruan, and M. J. Comb. 2000. BAD Ser-155 phosphorylation regulates BAD/Bcl-XL interaction and cell survival. J. Biol. Chem. 275:25865-25869.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25865-25869
    • Tan, Y.1    Demeter, M.R.2    Ruan, H.3    Comb, M.J.4
  • 34
    • 0033520937 scopus 로고    scopus 로고
    • p90(RSK) blocks Bad-mediated cell death via a protein kinase C-dependent pathway
    • Tan, Y., H. Ruan, M. R. Demeter, and M. J. Comb. 1999. p90(RSK) blocks Bad-mediated cell death via a protein kinase C-dependent pathway. J. Biol. Chem. 274:34859-34867.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34859-34867
    • Tan, Y.1    Ruan, H.2    Demeter, M.R.3    Comb, M.J.4
  • 35
    • 0036479325 scopus 로고    scopus 로고
    • 14-3-3 Proteins: Active cofactors in cellular regulation by serine/threonine phosphorylation
    • Tzivion, G., and J. Avruch. 2002. 14-3-3 proteins: active cofactors in cellular regulation by serine/threonine phosphorylation. J. Biol. Chem. 277:3061-3064.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3061-3064
    • Tzivion, G.1    Avruch, J.2
  • 36
    • 0034650872 scopus 로고    scopus 로고
    • 14-3-3 Isotypes facilitate coupling of protein kinase C-zeta to Raf-1: Negative regulation by 14-3-3 phosphorylation
    • Van Der Hoeven, P. C., J. C. Van Der Wal, P. Ruurs, M. C. Van Dijk, and J. Van Blitterswijk. 2000. Blitterswijk. 2000. 14-3-3 isotypes facilitate coupling of protein kinase C-zeta to Raf-1: negative regulation by 14-3-3 phosphorylation. Biochem. J. 345:297-306.
    • (2000) Biochem. J. , vol.345 , pp. 297-306
    • Van Der Hoeven, P.C.1    Van Der Wal, J.C.2    Ruurs, P.3    Van Dijk, M.C.4    Van Blitterswijk, J.5
  • 37
    • 0035895944 scopus 로고    scopus 로고
    • Phosphorylation of the proapoptotic protein BIK: Mapping of phosphorylation sites and effect on apoptosis
    • Verma, S., L. J. Zhao, and G. Chinnadurai. 2001. Phosphorylation of the proapoptotic protein BIK: mapping of phosphorylation sites and effect on apoptosis. J. Biol. Chem. 276:4671-4676.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4671-4676
    • Verma, S.1    Zhao, L.J.2    Chinnadurai, G.3
  • 38
    • 0030720062 scopus 로고    scopus 로고
    • Fostriecin, an antitumor antibiotic with inhibitory activity against serine/threonine protein phosphalases types 1 (PP1) and 2A (PP2A), is highly selective for PP2A
    • Walsh, A. H., A. Cheng, and R. E. Honkanen. 1997. Fostriecin, an antitumor antibiotic with inhibitory activity against serine/threonine protein phosphalases types 1 (PP1) and 2A (PP2A), is highly selective for PP2A. FEBS Lett. 416:230-234.
    • (1997) FEBS Lett. , vol.416 , pp. 230-234
    • Walsh, A.H.1    Cheng, A.2    Honkanen, R.E.3
  • 39
    • 0033592326 scopus 로고    scopus 로고
    • Isolation of high-affinity peptide antagonists of 14-3-3 proteins by phage display
    • Wang, B., H. Yang, Y. C. Liu, T. Jelinek, L. Zhang, E. Ruoslahti, and H. Fu. 1999. Isolation of high-affinity peptide antagonists of 14-3-3 proteins by phage display. Biochemistry 38:12499-12504.
    • (1999) Biochemistry , vol.38 , pp. 12499-12504
    • Wang, B.1    Yang, H.2    Liu, Y.C.3    Jelinek, T.4    Zhang, L.5    Ruoslahti, E.6    Fu, H.7
  • 41
    • 0037138389 scopus 로고    scopus 로고
    • How do 14-3-3 proteins work? Gatekeeper phosphorylation and the molecular anvil hypothesis
    • Yaffe, M. B. 2002. How do 14-3-3 proteins work? Gatekeeper phosphorylation and the molecular anvil hypothesis. FEBS Lett. 513:53-57.
    • (2002) FEBS Lett. , vol.513 , pp. 53-57
    • Yaffe, M.B.1
  • 43
    • 0028809209 scopus 로고
    • Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death
    • Yang, E., J. Zha, J. Jockel, L. H. Boise, C. B. Thompson, and S. J. Korsmeyer. 1995. Bad, a heterodimeric partner for Bcl-XL 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
  • 44
    • 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(L)
    • Zha, J., H. Harada, E. Yang, J. Jockel, and S. J. Korsmeyer. 1996. Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L). Cell 87:619-628.
    • (1996) Cell , vol.87 , pp. 619-628
    • Zha, J.1    Harada, H.2    Yang, E.3    Jockel, J.4    Korsmeyer, S.J.5
  • 45
    • 0034637606 scopus 로고    scopus 로고
    • Growth factors inactivate the cell death promoter BAD by phosphorylation of its BH3 domain on Ser155
    • Zhou, X. M., Y. Liu, G. Payne, R. J. Lutz, and T. Chittenden. 2000. Growth factors inactivate the cell death promoter BAD by phosphorylation of its BH3 domain on Ser155. J. Biol. Chem. 275:25046-25051.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25046-25051
    • Zhou, X.M.1    Liu, Y.2    Payne, G.3    Lutz, R.J.4    Chittenden, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.