메뉴 건너뛰기




Volumn 1810, Issue 2, 2011, Pages 162-169

Pore-forming activity of BAD is regulated by specific phosphorylation and structural transitions of the C-terminal part

Author keywords

Bcl 2 proteins; Channel; Phosphorylation; Protein interaction; Structure

Indexed keywords

BH3 PROTEIN; LIPID BINDING DOMAIN 2 PROTEIN; LIPID BINDING PROTEIN; PROTEIN BAD; SERINE; UNCLASSIFIED DRUG;

EID: 78649789742     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2010.11.002     Document Type: Article
Times cited : (6)

References (49)
  • 1
    • 19244365798 scopus 로고    scopus 로고
    • The domains of apoptosis: A genomics perspective
    • J.C. Reed, K.S. Doctor, and A. Godzik The domains of apoptosis: a genomics perspective Sci. STKE 2004 (2004) re9.
    • (2004) Sci. STKE
    • Reed, J.C.1    Doctor, K.S.2    Godzik, A.3
  • 2
    • 0842281645 scopus 로고    scopus 로고
    • Cell death: Critical control points
    • N.N. Danial, and S.J. Korsmeyer Cell death: critical control points Cell 116 2004 205 219
    • (2004) Cell , vol.116 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 3
    • 73349091842 scopus 로고    scopus 로고
    • The role of mitochondria in apoptosis*
    • C. Wang, and R.J. Youle The role of mitochondria in apoptosis* Annu. Rev. Genet. 43 2009 95 118
    • (2009) Annu. Rev. Genet. , vol.43 , pp. 95-118
    • Wang, C.1    Youle, R.J.2
  • 4
    • 37549048249 scopus 로고    scopus 로고
    • The BCL-2 protein family: Opposing activities that mediate cell death
    • R.J. Youle, and A. Strasser The BCL-2 protein family: opposing activities that mediate cell death Nat. Rev. Mol. Cell Biol. 9 2008 47 59
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2
  • 5
    • 68149107692 scopus 로고    scopus 로고
    • BAD: Undertaker by night, candyman by day
    • N.N. Danial BAD: undertaker by night, candyman by day Oncogene 27 Suppl 1 2008 S53 S70
    • (2008) Oncogene , vol.27 , Issue.SUPPL. 1
    • Danial, N.N.1
  • 6
    • 0032575688 scopus 로고    scopus 로고
    • The Bcl-2 protein family: Arbiters of cell survival
    • J.M. Adams, and S. Cory The Bcl-2 protein family: arbiters of cell survival Science 281 1998 1322 1326
    • (1998) Science , vol.281 , pp. 1322-1326
    • Adams, J.M.1    Cory, S.2
  • 7
    • 0033179760 scopus 로고    scopus 로고
    • BCL-2 family members and the mitochondria in apoptosis
    • A. Gross, J.M. McDonnell, and S.J. Korsmeyer BCL-2 family members and the mitochondria in apoptosis Genes Dev. 13 1999 1899 1911
    • (1999) Genes Dev. , vol.13 , pp. 1899-1911
    • Gross, A.1    McDonnell, J.M.2    Korsmeyer, S.J.3
  • 8
    • 0034644508 scopus 로고    scopus 로고
    • Insights into programmed cell death through structural biology
    • S.W. Fesik Insights into programmed cell death through structural biology Cell 103 2000 273 282
    • (2000) Cell , vol.103 , pp. 273-282
    • Fesik, S.W.1
  • 10
    • 0028809209 scopus 로고
    • Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death
    • E. Yang, J. Zha, J. Jockel, L.H. Boise, C.B. Thompson, and S.J. Korsmeyer Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death Cell 80 1995 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
  • 11
  • 12
    • 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)
    • J. Zha, H. Harada, E. Yang, J. Jockel, and S.J. Korsmeyer Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L) Cell 87 1996 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
  • 13
    • 0036533631 scopus 로고    scopus 로고
    • Segregation of Bad from lipid rafts is implicated in the induction of apoptosis
    • V. Ayllon, A. Fleischer, X. Cayla, A. Garcia, and A. Rebollo Segregation of Bad from lipid rafts is implicated in the induction of apoptosis J. Immunol. 168 2002 3387 3393
    • (2002) J. Immunol. , vol.168 , pp. 3387-3393
    • Ayllon, V.1    Fleischer, A.2    Cayla, X.3    Garcia, A.4    Rebollo, A.5
  • 14
    • 0033635235 scopus 로고    scopus 로고
    • 14-3-3 proteins and survival kinases cooperate to inactivate BAD by BH3 domain phosphorylation
    • S.R. Datta, A. Katsov, L. Hu, A. Petros, S.W. Fesik, M.B. Yaffe, and M.E. Greenberg 14-3-3 proteins and survival kinases cooperate to inactivate BAD by BH3 domain phosphorylation Mol. Cell 6 2000 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
  • 15
    • 0037458090 scopus 로고    scopus 로고
    • Apoptosis: Mitochondrial membrane permeabilization-the (w)hole story?
    • N. Zamzami, and G. Kroemer Apoptosis: mitochondrial membrane permeabilization-the (w)hole story? Curr. Biol. 13 2003 R71 R73
    • (2003) Curr. Biol. , vol.13
    • Zamzami, N.1    Kroemer, G.2
  • 16
    • 33750619845 scopus 로고    scopus 로고
    • How do Bax and Bak lead to permeabilization of the outer mitochondrial membrane?
    • A. Antignani, and R.J. Youle How do Bax and Bak lead to permeabilization of the outer mitochondrial membrane? Curr. Opin. Cell Biol. 18 2006 685 689
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 685-689
    • Antignani, A.1    Youle, R.J.2
  • 25
    • 78650680262 scopus 로고    scopus 로고
    • Can BAD pores be good? New insights from examining BAD as a target of RAF kinases
    • L. Polzien, R. Benz, and U.R. Rapp Can BAD pores be good? New insights from examining BAD as a target of RAF kinases Adv. Enzyme Regul. 2009
    • (2009) Adv. Enzyme Regul.
    • Polzien, L.1    Benz, R.2    Rapp, U.R.3
  • 26
    • 0026872512 scopus 로고
    • Studies on human porin. VII. The channel properties of the human B-lymphocyte membrane-derived "porin 31HL" are similar to those of mitochondrial porins
    • R. Benz, E. Maier, F.P. Thinnes, H. Gotz, and N. Hilschmann Studies on human porin. VII. The channel properties of the human B-lymphocyte membrane-derived "Porin 31HL" are similar to those of mitochondrial porins Biol. Chem. Hoppe Seyler 373 1992 295 303
    • (1992) Biol. Chem. Hoppe Seyler , vol.373 , pp. 295-303
    • Benz, R.1    Maier, E.2    Thinnes, F.P.3    Gotz, H.4    Hilschmann, N.5
  • 27
    • 0028341536 scopus 로고
    • Permeation of hydrophilic solutes through mitochondrial outer membranes: Review on mitochondrial porins
    • R. Benz Permeation of hydrophilic solutes through mitochondrial outer membranes: review on mitochondrial porins Biochim. Biophys. Acta 1197 1994 167 196
    • (1994) Biochim. Biophys. Acta , vol.1197 , pp. 167-196
    • Benz, R.1
  • 28
    • 0040185619 scopus 로고    scopus 로고
    • Study of the secondary structure of the C-terminal domain of the antiapoptotic protein bcl-2 and its interaction with model membranes
    • M. del Mar Martinez-Senac, S. Corbalan-Garcia, and J.C. Gomez-Fernandez Study of the secondary structure of the C-terminal domain of the antiapoptotic protein bcl-2 and its interaction with model membranes Biochemistry 39 2000 7744 7752
    • (2000) Biochemistry , vol.39 , pp. 7744-7752
    • Del Mar Martinez-Senac, M.1    Corbalan-Garcia, S.2    Gomez-Fernandez, J.C.3
  • 29
    • 0035928830 scopus 로고    scopus 로고
    • Conformation of the C-terminal domain of the pro-apoptotic protein Bax and mutants and its interaction with membranes
    • M. del Mar Martinez-Senac, S. Corbalan-Garcia, and J.C. Gomez-Fernandez Conformation of the C-terminal domain of the pro-apoptotic protein Bax and mutants and its interaction with membranes Biochemistry 40 2001 9983 9992
    • (2001) Biochemistry , vol.40 , pp. 9983-9992
    • Del Mar Martinez-Senac, M.1    Corbalan-Garcia, S.2    Gomez-Fernandez, J.C.3
  • 30
    • 0036220239 scopus 로고    scopus 로고
    • The structure of the C-terminal domain of the pro-apoptotic protein Bak and its interaction with model membranes
    • M. Martinez-Senac Mdel, S. Corbalan-Garcia, and J.C. Gomez-Fernandez The structure of the C-terminal domain of the pro-apoptotic protein Bak and its interaction with model membranes Biophys. J. 82 2002 233 243
    • (2002) Biophys. J. , vol.82 , pp. 233-243
    • Martinez-Senac Mdel, M.1    Corbalan-Garcia, S.2    Gomez-Fernandez, J.C.3
  • 33
    • 59649084902 scopus 로고    scopus 로고
    • Molecular modeling of human BAD and its interaction with PKAc or PP1c
    • J. Yang Molecular modeling of human BAD and its interaction with PKAc or PP1c J. Theor. Biol. 257 2009 159 169
    • (2009) J. Theor. Biol. , vol.257 , pp. 159-169
    • Yang, J.1
  • 34
    • 33845486323 scopus 로고    scopus 로고
    • Bim, Bad and Bmf: Intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets
    • M.G. Hinds, C. Smits, R. Fredericks-Short, J.M. Risk, M. Bailey, D.C. Huang, and C.L. Day Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets Cell Death Differ. 14 2007 128 136
    • (2007) Cell Death Differ. , vol.14 , pp. 128-136
    • Hinds, M.G.1    Smits, C.2    Fredericks-Short, R.3    Risk, J.M.4    Bailey, M.5    Huang, D.C.6    Day, C.L.7
  • 35
    • 50649121583 scopus 로고    scopus 로고
    • Solution structure of the integral human membrane protein VDAC-1 in detergent micelles
    • S. Hiller, R.G. Garces, T.J. Malia, V.Y. Orekhov, M. Colombini, and G. Wagner Solution structure of the integral human membrane protein VDAC-1 in detergent micelles Science 321 2008 1206 1210
    • (2008) Science , vol.321 , pp. 1206-1210
    • Hiller, S.1    Garces, R.G.2    Malia, T.J.3    Orekhov, V.Y.4    Colombini, M.5    Wagner, G.6
  • 36
    • 34247497716 scopus 로고    scopus 로고
    • Embedded together: The life and death consequences of interaction of the Bcl-2 family with membranes
    • B. Leber, J. Lin, and D.W. Andrews Embedded together: the life and death consequences of interaction of the Bcl-2 family with membranes Apoptosis 12 2007 897 911
    • (2007) Apoptosis , vol.12 , pp. 897-911
    • Leber, B.1    Lin, J.2    Andrews, D.W.3
  • 37
    • 2942625430 scopus 로고    scopus 로고
    • Bcl-x(L) sequesters its C-terminal membrane anchor in soluble, cytosolic homodimers
    • S.Y. Jeong, B. Gaume, Y.J. Lee, Y.T. Hsu, S.W. Ryu, S.H. Yoon, and R.J. Youle Bcl-x(L) sequesters its C-terminal membrane anchor in soluble, cytosolic homodimers EMBO J. 23 2004 2146 2155
    • (2004) EMBO J. , vol.23 , pp. 2146-2155
    • Jeong, S.Y.1    Gaume, B.2    Lee, Y.J.3    Hsu, Y.T.4    Ryu, S.W.5    Yoon, S.H.6    Youle, R.J.7
  • 38
    • 0029116916 scopus 로고
    • The mitochondrial permeability transition
    • M. Zoratti, and I. Szabo The mitochondrial permeability transition Biochim. Biophys. Acta 1241 1995 139 176
    • (1995) Biochim. Biophys. Acta , vol.1241 , pp. 139-176
    • Zoratti, M.1    Szabo, I.2
  • 39
    • 0029983059 scopus 로고    scopus 로고
    • Inhibitors of permeability transition interfere with the disruption of the mitochondrial transmembrane potential during apoptosis
    • N. Zamzami, P. Marchetti, M. Castedo, T. Hirsch, S.A. Susin, B. Masse, and G. Kroemer Inhibitors of permeability transition interfere with the disruption of the mitochondrial transmembrane potential during apoptosis FEBS Lett. 384 1996 53 57
    • (1996) FEBS Lett. , vol.384 , pp. 53-57
    • Zamzami, N.1    Marchetti, P.2    Castedo, M.3    Hirsch, T.4    Susin, S.A.5    Masse, B.6    Kroemer, G.7
  • 41
    • 59649092928 scopus 로고    scopus 로고
    • Bad targets the permeability transition pore independent of Bax or Bak to switch between Ca2 + -dependent cell survival and death
    • S.S. Roy, M. Madesh, E. Davies, B. Antonsson, N. Danial, and G. Hajnoczky Bad targets the permeability transition pore independent of Bax or Bak to switch between Ca2 + -dependent cell survival and death Mol. Cell 33 2009 377 388
    • (2009) Mol. Cell , vol.33 , pp. 377-388
    • Roy, S.S.1    Madesh, M.2    Davies, E.3    Antonsson, B.4    Danial, N.5    Hajnoczky, G.6
  • 42
    • 0036792001 scopus 로고    scopus 로고
    • Mitochondrial respiratory control is lost during growth factor deprivation
    • E. Gottlieb, S.M. Armour, and C.B. Thompson Mitochondrial respiratory control is lost during growth factor deprivation Proc. Natl Acad. Sci. USA 99 2002 12801 12806
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 12801-12806
    • Gottlieb, E.1    Armour, S.M.2    Thompson, C.B.3
  • 43
    • 0033258120 scopus 로고    scopus 로고
    • Bcl-2 proteins: Regulators of apoptosis or of mitochondrial homeostasis?
    • M.G. Vander Heiden, and C.B. Thompson Bcl-2 proteins: regulators of apoptosis or of mitochondrial homeostasis? Nat. Cell Biol. 1 1999 E209 E216
    • (1999) Nat. Cell Biol. , vol.1
    • Vander Heiden, M.G.1    Thompson, C.B.2
  • 45
    • 12744278057 scopus 로고    scopus 로고
    • Bad-dependent rafts alteration is a consequence of an early intracellular signal triggered by interleukin-4 deprivation
    • A. Fleischer, A. Ghadiri, F. Dessauge, M. Duhamel, X. Cayla, A. Garcia, and A. Rebollo Bad-dependent rafts alteration is a consequence of an early intracellular signal triggered by interleukin-4 deprivation Mol. Cancer Res. 2 2004 674 684
    • (2004) Mol. Cancer Res. , vol.2 , pp. 674-684
    • Fleischer, A.1    Ghadiri, A.2    Dessauge, F.3    Duhamel, M.4    Cayla, X.5    Garcia, A.6    Rebollo, A.7
  • 47
    • 0037025377 scopus 로고    scopus 로고
    • Associations of B- and C-Raf with cholesterol, phosphatidylserine, and lipid second messengers: Preferential binding of Raf to artificial lipid rafts
    • M. Hekman, H. Hamm, A.V. Villar, B. Bader, J. Kuhlmann, J. Nickel, and U.R. Rapp Associations of B- and C-Raf with cholesterol, phosphatidylserine, and lipid second messengers: preferential binding of Raf to artificial lipid rafts J. Biol. Chem. 277 2002 24090 24102
    • (2002) J. Biol. Chem. , vol.277 , pp. 24090-24102
    • Hekman, M.1    Hamm, H.2    Villar, A.V.3    Bader, B.4    Kuhlmann, J.5    Nickel, J.6    Rapp, U.R.7
  • 49
    • 34548124682 scopus 로고    scopus 로고
    • BAD association with membranes is regulated by Raf kinases and association with 14-3-3 proteins
    • U.R. Rapp, A. Fischer, U.E. Rennefahrt, M. Hekman, and S. Albert BAD association with membranes is regulated by Raf kinases and association with 14-3-3 proteins Adv. Enzyme Regul. 47 2007 281 285
    • (2007) Adv. Enzyme Regul. , vol.47 , pp. 281-285
    • Rapp, U.R.1    Fischer, A.2    Rennefahrt, U.E.3    Hekman, M.4    Albert, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.