메뉴 건너뛰기




Volumn 152, Issue 3, 2013, Pages 519-531

Bax crystal structures reveal how BH3 domains activate Bax and nucleate its oligomerization to induce apoptosis

Author keywords

[No Author keywords available]

Indexed keywords

BH3 PROTEIN; DETERGENT; HOMODIMER; PROTEIN BAX;

EID: 84873307384     PISSN: 00928674     EISSN: 10974172     Source Type: Journal    
DOI: 10.1016/j.cell.2012.12.031     Document Type: Article
Times cited : (472)

References (69)
  • 4
    • 4143058003 scopus 로고    scopus 로고
    • The evolving role of 3D domain swapping in proteins
    • M.J. Bennett, and D. Eisenberg The evolving role of 3D domain swapping in proteins Structure 12 2004 1339 1341
    • (2004) Structure , vol.12 , pp. 1339-1341
    • Bennett, M.J.1    Eisenberg, D.2
  • 8
    • 0037087706 scopus 로고    scopus 로고
    • The expression of a new variant of the pro-apoptotic molecule Bax, Baxpsi, is correlated with an increased survival of glioblastoma multiforme patients
    • P.F. Cartron, L. Oliver, S. Martin, C. Moreau, M.T. LeCabellec, P. Jezequel, K. Meflah, and F.M. Vallette The expression of a new variant of the pro-apoptotic molecule Bax, Baxpsi, is correlated with an increased survival of glioblastoma multiforme patients Hum. Mol. Genet. 11 2002 675 687
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 675-687
    • Cartron, P.F.1    Oliver, L.2    Martin, S.3    Moreau, C.4    Lecabellec, M.T.5    Jezequel, P.6    Meflah, K.7    Vallette, F.M.8
  • 9
    • 33646354381 scopus 로고    scopus 로고
    • Mitochondria primed by death signals determine cellular addiction to antiapoptotic BCL-2 family members
    • M. Certo, V. Del Gaizo Moore, M. Nishino, G. Wei, S. Korsmeyer, S.A. Armstrong, and A. Letai Mitochondria primed by death signals determine cellular addiction to antiapoptotic BCL-2 family members Cancer Cell 9 2006 351 365
    • (2006) Cancer Cell , vol.9 , pp. 351-365
    • Certo, M.1    Del Gaizo Moore, V.2    Nishino, M.3    Wei, G.4    Korsmeyer, S.5    Armstrong, S.A.6    Letai, A.7
  • 10
    • 79953192533 scopus 로고    scopus 로고
    • Mutation to Bax beyond the BH3 domain disrupts interactions with pro-survival proteins and promotes apoptosis
    • P.E. Czabotar, E.F. Lee, G.V. Thompson, A.Z. Wardak, W.D. Fairlie, and P.M. Colman Mutation to Bax beyond the BH3 domain disrupts interactions with pro-survival proteins and promotes apoptosis J. Biol. Chem. 286 2011 7123 7131
    • (2011) J. Biol. Chem. , vol.286 , pp. 7123-7131
    • Czabotar, P.E.1    Lee, E.F.2    Thompson, G.V.3    Wardak, A.Z.4    Fairlie, W.D.5    Colman, P.M.6
  • 11
    • 79960235245 scopus 로고    scopus 로고
    • Transient binding of an activator BH3 domain to the Bak BH3-binding groove initiates Bak oligomerization
    • H. Dai, A. Smith, X.W. Meng, P.A. Schneider, Y.P. Pang, and S.H. Kaufmann Transient binding of an activator BH3 domain to the Bak BH3-binding groove initiates Bak oligomerization J. Cell Biol. 194 2011 39 48
    • (2011) J. Cell Biol. , vol.194 , pp. 39-48
    • Dai, H.1    Smith, A.2    Meng, X.W.3    Schneider, P.A.4    Pang, Y.P.5    Kaufmann, S.H.6
  • 12
    • 43049105074 scopus 로고    scopus 로고
    • To trigger apoptosis, Bak exposes its BH3 domain and homodimerizes via BH3:groove interactions
    • G. Dewson, T. Kratina, H.W. Sim, H. Puthalakath, J.M. Adams, P.M. Colman, and R.M. Kluck To trigger apoptosis, Bak exposes its BH3 domain and homodimerizes via BH3:groove interactions Mol. Cell 30 2008 369 380
    • (2008) Mol. Cell , vol.30 , pp. 369-380
    • Dewson, G.1    Kratina, T.2    Sim, H.W.3    Puthalakath, H.4    Adams, J.M.5    Colman, P.M.6    Kluck, R.M.7
  • 13
    • 70449941949 scopus 로고    scopus 로고
    • Bak activation for apoptosis involves oligomerization of dimers via their alpha6 helices
    • G. Dewson, T. Kratina, P. Czabotar, C.L. Day, J.M. Adams, and R.M. Kluck Bak activation for apoptosis involves oligomerization of dimers via their alpha6 helices Mol. Cell 36 2009 696 703
    • (2009) Mol. Cell , vol.36 , pp. 696-703
    • Dewson, G.1    Kratina, T.2    Czabotar, P.3    Day, C.L.4    Adams, J.M.5    Kluck, R.M.6
  • 15
    • 33747818007 scopus 로고    scopus 로고
    • CASTp: Computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues
    • J. Dundas, Z. Ouyang, J. Tseng, A. Binkowski, Y. Turpaz, and J. Liang CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues Nucleic Acids Res. 34 Web Server issue 2006 W116 W118
    • (2006) Nucleic Acids Res. , vol.34
    • Dundas, J.1    Ouyang, Z.2    Tseng, J.3    Binkowski, A.4    Turpaz, Y.5    Liang, J.6
  • 18
    • 0347481136 scopus 로고    scopus 로고
    • Transbilayer lipid diffusion promoted by Bax: Implications for apoptosis
    • R.F. Epand, J.C. Martinou, S. Montessuit, and R.M. Epand Transbilayer lipid diffusion promoted by Bax: implications for apoptosis Biochemistry 42 2003 14576 14582
    • (2003) Biochemistry , vol.42 , pp. 14576-14582
    • Epand, R.F.1    Martinou, J.C.2    Montessuit, S.3    Epand, R.M.4
  • 20
    • 58149299435 scopus 로고    scopus 로고
    • Baxbeta: A constitutively active human Bax isoform that is under tight regulatory control by the proteasomal degradation mechanism
    • N.Y. Fu, S.K. Sukumaran, S.Y. Kerk, and V.C. Yu Baxbeta: a constitutively active human Bax isoform that is under tight regulatory control by the proteasomal degradation mechanism Mol. Cell 33 2009 15 29
    • (2009) Mol. Cell , vol.33 , pp. 15-29
    • Fu, N.Y.1    Sukumaran, S.K.2    Kerk, S.Y.3    Yu, V.C.4
  • 21
    • 84856278457 scopus 로고    scopus 로고
    • Molecular view of the role of fusion peptides in promoting positive membrane curvature
    • M. Fuhrmans, and S.J. Marrink Molecular view of the role of fusion peptides in promoting positive membrane curvature J. Am. Chem. Soc. 134 2012 1543 1552
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 1543-1552
    • Fuhrmans, M.1    Marrink, S.J.2
  • 23
    • 78149449341 scopus 로고    scopus 로고
    • BH3-triggered structural reorganization drives the activation of proapoptotic BAX
    • E. Gavathiotis, D.E. Reyna, M.L. Davis, G.H. Bird, and L.D. Walensky BH3-triggered structural reorganization drives the activation of proapoptotic BAX Mol. Cell 40 2010 481 492
    • (2010) Mol. Cell , vol.40 , pp. 481-492
    • Gavathiotis, E.1    Reyna, D.E.2    Davis, M.L.3    Bird, G.H.4    Walensky, L.D.5
  • 24
    • 34547629939 scopus 로고    scopus 로고
    • A three-helix homo-oligomerization domain containing BH3 and BH1 is responsible for the apoptotic activity of Bax
    • N.M. George, J.J. Evans, and X. Luo A three-helix homo-oligomerization domain containing BH3 and BH1 is responsible for the apoptotic activity of Bax Genes Dev. 21 2007 1937 1948
    • (2007) Genes Dev. , vol.21 , pp. 1937-1948
    • George, N.M.1    Evans, J.J.2    Luo, X.3
  • 26
    • 0031007644 scopus 로고    scopus 로고
    • Nonionic detergents induce dimerization among members of the Bcl-2 family
    • Y.T. Hsu, and R.J. Youle Nonionic detergents induce dimerization among members of the Bcl-2 family J. Biol. Chem. 272 1997 13829 13834
    • (1997) J. Biol. Chem. , vol.272 , pp. 13829-13834
    • Hsu, Y.T.1    Youle, R.J.2
  • 27
    • 0032562796 scopus 로고    scopus 로고
    • Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations
    • Y.T. Hsu, and R.J. Youle Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations J. Biol. Chem. 273 1998 10777 10783
    • (1998) J. Biol. Chem. , vol.273 , pp. 10777-10783
    • Hsu, Y.T.1    Youle, R.J.2
  • 28
    • 0030963602 scopus 로고    scopus 로고
    • Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis
    • Y.T. Hsu, K.G. Wolter, and R.J. Youle Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis Proc. Natl. Acad. Sci. USA 94 1997 3668 3672
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3668-3672
    • Hsu, Y.T.1    Wolter, K.G.2    Youle, R.J.3
  • 33
    • 13944277343 scopus 로고    scopus 로고
    • BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly
    • T. Kuwana, L. Bouchier-Hayes, J.E. Chipuk, C. Bonzon, B.A. Sullivan, D.R. Green, and D.D. Newmeyer BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly Mol. Cell 17 2005 525 535
    • (2005) Mol. Cell , vol.17 , pp. 525-535
    • Kuwana, T.1    Bouchier-Hayes, L.2    Chipuk, J.E.3    Bonzon, C.4    Sullivan, B.A.5    Green, D.R.6    Newmeyer, D.D.7
  • 36
    • 65349185520 scopus 로고    scopus 로고
    • Puma strikes Bax
    • A. Letai Puma strikes Bax J. Cell Biol. 185 2009 189 191
    • (2009) J. Cell Biol. , vol.185 , pp. 189-191
    • Letai, A.1
  • 37
    • 0036728834 scopus 로고    scopus 로고
    • Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics
    • A. Letai, M.C. Bassik, L.D. Walensky, M.D. Sorcinelli, S. Weiler, and S.J. Korsmeyer Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics Cancer Cell 2 2002 183 192
    • (2002) Cancer Cell , vol.2 , pp. 183-192
    • Letai, A.1    Bassik, M.C.2    Walensky, L.D.3    Sorcinelli, M.D.4    Weiler, S.5    Korsmeyer, S.J.6
  • 38
    • 0042220409 scopus 로고    scopus 로고
    • The structure of a Bcl-xL/Bim fragment complex: Implications for Bim function
    • X. Liu, S. Dai, Y. Zhu, P. Marrack, and J.W. Kappler The structure of a Bcl-xL/Bim fragment complex: implications for Bim function Immunity 19 2003 341 352
    • (2003) Immunity , vol.19 , pp. 341-352
    • Liu, X.1    Dai, S.2    Zhu, Y.3    Marrack, P.4    Kappler, J.W.5
  • 40
    • 57149135309 scopus 로고    scopus 로고
    • Membrane binding by tBid initiates an ordered series of events culminating in membrane permeabilization by Bax
    • J.F. Lovell, L.P. Billen, S. Bindner, A. Shamas-Din, C. Fradin, B. Leber, and D.W. Andrews Membrane binding by tBid initiates an ordered series of events culminating in membrane permeabilization by Bax Cell 135 2008 1074 1084
    • (2008) Cell , vol.135 , pp. 1074-1084
    • Lovell, J.F.1    Billen, L.P.2    Bindner, S.3    Shamas-Din, A.4    Fradin, C.5    Leber, B.6    Andrews, D.W.7
  • 43
    • 66649132042 scopus 로고    scopus 로고
    • The structure of a cytolytic α-helical toxin pore reveals its assembly mechanism
    • M. Mueller, U. Grauschopf, T. Maier, R. Glockshuber, and N. Ban The structure of a cytolytic α-helical toxin pore reveals its assembly mechanism Nature 459 2009 726 730
    • (2009) Nature , vol.459 , pp. 726-730
    • Mueller, M.1    Grauschopf, U.2    Maier, T.3    Glockshuber, R.4    Ban, N.5
  • 44
    • 0033522391 scopus 로고    scopus 로고
    • Conformation of the Bax C-terminus regulates subcellular location and cell death
    • A. Nechushtan, C.L. Smith, Y.T. Hsu, and R.J. Youle Conformation of the Bax C-terminus regulates subcellular location and cell death EMBO J. 18 1999 2330 2341
    • (1999) EMBO J. , vol.18 , pp. 2330-2341
    • Nechushtan, A.1    Smith, C.L.2    Hsu, Y.T.3    Youle, R.J.4
  • 46
    • 77956523192 scopus 로고    scopus 로고
    • Conformational changes in BAK, a pore-forming proapoptotic Bcl-2 family member, upon membrane insertion and direct evidence for the existence of BH3-BH3 contact interface in BAK homo-oligomers
    • K.J. Oh, P. Singh, K. Lee, K. Foss, S. Lee, M. Park, S. Lee, S. Aluvila, M. Park, and P. Singh Conformational changes in BAK, a pore-forming proapoptotic Bcl-2 family member, upon membrane insertion and direct evidence for the existence of BH3-BH3 contact interface in BAK homo-oligomers J. Biol. Chem. 285 2010 28924 28937
    • (2010) J. Biol. Chem. , vol.285 , pp. 28924-28937
    • Oh, K.J.1    Singh, P.2    Lee, K.3    Foss, K.4    Lee, S.5    Park, M.6    Lee, S.7    Aluvila, S.8    Park, M.9    Singh, P.10
  • 47
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode. Macromolecular Crystallography, Pt
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode. Macromolecular Crystallography, Pt Methods Enzymol. 276 1997 307 326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 48
    • 84859753178 scopus 로고    scopus 로고
    • Bak conformational changes induced by ligand binding: Insight into BH3 domain binding and Bak homo-oligomerization
    • 10.1038/srep00257 Published online February 10, 2012
    • Y.P. Pang, H. Dai, A. Smith, X.W. Meng, P.A. Schneider, and S.H. Kaufmann Bak conformational changes induced by ligand binding: insight into BH3 domain binding and Bak homo-oligomerization Sci. Rep. 2012 10.1038/srep00257 Published online February 10, 2012
    • (2012) Sci. Rep.
    • Pang, Y.P.1    Dai, H.2    Smith, A.3    Meng, X.W.4    Schneider, P.A.5    Kaufmann, S.H.6
  • 49
    • 9244241054 scopus 로고    scopus 로고
    • Pore-forming protein toxins: From structure to function
    • M.W. Parker, and S.C. Feil Pore-forming protein toxins: from structure to function Prog. Biophys. Mol. Biol. 88 2005 91 142
    • (2005) Prog. Biophys. Mol. Biol. , vol.88 , pp. 91-142
    • Parker, M.W.1    Feil, S.C.2
  • 50
    • 56249132688 scopus 로고    scopus 로고
    • Structure of transmembrane pore induced by Bax-derived peptide: Evidence for lipidic pores
    • S. Qian, W. Wang, L. Yang, and H.W. Huang Structure of transmembrane pore induced by Bax-derived peptide: evidence for lipidic pores Proc. Natl. Acad. Sci. USA 105 2008 17379 17383
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 17379-17383
    • Qian, S.1    Wang, W.2    Yang, L.3    Huang, H.W.4
  • 51
    • 77955463665 scopus 로고    scopus 로고
    • Nonconsecutive disulfide bond formation in an essential integral outer membrane protein
    • N. Ruiz, S.S. Chng, A. Hiniker, D. Kahne, and T.J. Silhavy Nonconsecutive disulfide bond formation in an essential integral outer membrane protein Proc. Natl. Acad. Sci. USA 107 2010 12245 12250
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 12245-12250
    • Ruiz, N.1    Chng, S.S.2    Hiniker, A.3    Kahne, D.4    Silhavy, T.J.5
  • 53
    • 0033713002 scopus 로고    scopus 로고
    • Structure of Bax: Coregulation of dimer formation and intracellular localization
    • M. Suzuki, R.J. Youle, and N. Tjandra Structure of Bax: coregulation of dimer formation and intracellular localization Cell 103 2000 645 654
    • (2000) Cell , vol.103 , pp. 645-654
    • Suzuki, M.1    Youle, R.J.2    Tjandra, N.3
  • 56
    • 33645978129 scopus 로고    scopus 로고
    • The mechanism of pore formation by bacterial toxins
    • S.J. Tilley, and H.R. Saibil The mechanism of pore formation by bacterial toxins Curr. Opin. Struct. Biol. 16 2006 230 236
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 230-236
    • Tilley, S.J.1    Saibil, H.R.2
  • 57
    • 0031660082 scopus 로고    scopus 로고
    • Mutagenesis of the BH3 domain of BAX identifies residues critical for dimerization and killing
    • K. Wang, A. Gross, G. Waksman, and S.J. Korsmeyer Mutagenesis of the BH3 domain of BAX identifies residues critical for dimerization and killing Mol. Cell. Biol. 18 1998 6083 6089
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6083-6089
    • Wang, K.1    Gross, A.2    Waksman, G.3    Korsmeyer, S.J.4
  • 61
    • 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
  • 63
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • C. Bartels, T.H. Xia, M. Billeter, P. Güntert, and K. Wüthrich The program XEASY for computer-supported NMR spectral analysis of biological macromolecules J. Biomol. NMR 6 1995 1 10
    • (1995) J. Biomol. NMR , vol.6 , pp. 1-10
    • Bartels, C.1    Xia, T.H.2    Billeter, M.3    Güntert, P.4    Wüthrich, K.5
  • 64
    • 84861425552 scopus 로고    scopus 로고
    • Linking crystallographic model and data quality
    • P.A. Karplus, and K. Diederichs Linking crystallographic model and data quality Science 336 2012 1030 1033
    • (2012) Science , vol.336 , pp. 1030-1033
    • Karplus, P.A.1    Diederichs, K.2
  • 65
    • 52149085903 scopus 로고    scopus 로고
    • EGL-1 BH3 mutants reveal the importance of protein levels and target affinity for cell-killing potency
    • E.F. Lee, L. Chen, H. Yang, P.M. Colman, D.C. Huang, and W.D. Fairlie EGL-1 BH3 mutants reveal the importance of protein levels and target affinity for cell-killing potency Cell Death Differ. 15 2008 1609 1618
    • (2008) Cell Death Differ. , vol.15 , pp. 1609-1618
    • Lee, E.F.1    Chen, L.2    Yang, H.3    Colman, P.M.4    Huang, D.C.5    Fairlie, W.D.6
  • 67
    • 0347722841 scopus 로고    scopus 로고
    • Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
    • M. Sattler, J. Schleucher, and C. Griesinger Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients Prog. Nucl. Magn. Reson. Spectrosc. 34 1999 93 158
    • (1999) Prog. Nucl. Magn. Reson. Spectrosc. , vol.34 , pp. 93-158
    • Sattler, M.1    Schleucher, J.2    Griesinger, C.3
  • 68
    • 34247527336 scopus 로고    scopus 로고
    • Mitochondrial permeabilization relies on BH3 ligands engaging multiple prosurvival Bcl-2 relatives, not Bak
    • R.T. Uren, G. Dewson, L. Chen, S.C. Coyne, D.C. Huang, J.M. Adams, and R.M. Kluck Mitochondrial permeabilization relies on BH3 ligands engaging multiple prosurvival Bcl-2 relatives, not Bak J. Cell Biol. 177 2007 277 287
    • (2007) J. Cell Biol. , vol.177 , pp. 277-287
    • Uren, R.T.1    Dewson, G.2    Chen, L.3    Coyne, S.C.4    Huang, D.C.5    Adams, J.M.6    Kluck, R.M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.