메뉴 건너뛰기




Volumn 289, Issue 47, 2014, Pages 32871-32882

Conformational rearrangements in the pro-apoptotic protein, bax, as it inserts into mitochondria: A cellular death switch

Author keywords

[No Author keywords available]

Indexed keywords

CELL DEATH; CELL MEMBRANES; CONFORMATIONS; ENERGY TRANSFER; FLUORESCENCE SPECTROSCOPY; MOLECULAR STRUCTURE; PROTEINS;

EID: 84911412568     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.593897     Document Type: Article
Times cited : (61)

References (36)
  • 1
    • 84890909335 scopus 로고    scopus 로고
    • Control of apoptosis by the BCL-2 protein family: Implications for physiology and therapy
    • Czabotar, P. E., Lessene, G., Strasser, A., and Adams, J. M. (2014) Control of apoptosis by the BCL-2 protein family: implications for physiology and therapy. Nat. Rev. Mol. Cell Biol. 15, 49-63
    • (2014) Nat. Rev. Mol. Cell Biol. , vol.15 , pp. 49-63
    • Czabotar, P.E.1    Lessene, G.2    Strasser, A.3    Adams, J.M.4
  • 2
    • 84882664898 scopus 로고    scopus 로고
    • Defining the role of the Bcl-2 family proteins in Huntington's disease
    • Sassone, J., Maraschi, A., Sassone, F., Silani, V., and Ciammola, A. (2013) Defining the role of the Bcl-2 family proteins in Huntington's disease. Cell Death Dis. 4, e772
    • (2013) Cell Death Dis. , vol.4 , pp. e772
    • Sassone, J.1    Maraschi, A.2    Sassone, F.3    Silani, V.4    Ciammola, A.5
  • 3
    • 3442886811 scopus 로고    scopus 로고
    • The pathophysiology of mitochondrial cell death
    • Green, D. R. (2004) The pathophysiology of mitochondrial cell death. Science 305, 626-629
    • (2004) Science , vol.305 , pp. 626-629
    • Green, D.R.1
  • 4
    • 0036716281 scopus 로고    scopus 로고
    • The bcl2 family: Regulators of the cellular life-or-death switch
    • Cory, S., and Adams, J. M. (2002) The bcl2 family: regulators of the cellular life-or-death switch. Nat. Rev. Cancer. 2, 647-656
    • (2002) Nat. Rev. Cancer. , vol.2 , pp. 647-656
    • Cory, S.1    Adams, J.M.2
  • 5
  • 6
    • 80051761743 scopus 로고    scopus 로고
    • The role of Bcl-2 and its pro-survival relatives in tumourigenesis and cancer therapy
    • Kelly, P. N., and Strasser, A. (2011) The role of Bcl-2 and its pro-survival relatives in tumourigenesis and cancer therapy. Cell Death Differ. 18, 1414-1424
    • (2011) Cell Death Differ. , vol.18 , pp. 1414-1424
    • Kelly, P.N.1    Strasser, A.2
  • 7
    • 37549048249 scopus 로고    scopus 로고
    • The BCL-2 protein family: Opposing activities that mediate cell death
    • Youle, R. J., and Strasser, A. (2008) The BCL-2 protein family: opposing activities that mediate cell death. Nat. Rev. Mol. Cell Biol. 9, 47-59
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2
  • 9
    • 84870990121 scopus 로고    scopus 로고
    • The secrets of the Bcl-2 family
    • García-Sáez, A. J. (2012) The secrets of the Bcl-2 family. Cell Death Differ. 19, 1733-1740
    • (2012) Cell Death Differ. , vol.19 , pp. 1733-1740
    • García-Sáez, A.J.1
  • 12
    • 84872298568 scopus 로고    scopus 로고
    • The C-terminal helix of Bcl-xL mediates Bax retrotranslocation from the mitochondria
    • Todt, F., Cakir, Z., Reichenbach, F., Youle, R. J., and Edlich, F. (2013) The C-terminal helix of Bcl-xL mediates Bax retrotranslocation from the mitochondria. Cell Death Differ. 20, 333-342
    • (2013) Cell Death Differ. , vol.20 , pp. 333-342
    • Todt, F.1    Cakir, Z.2    Reichenbach, F.3    Youle, R.J.4    Edlich, F.5
  • 13
    • 84896486413 scopus 로고    scopus 로고
    • Single color FRET based measurements of conformational changes of proteins resulting from translocation inside cells
    • Gahl, R. F., Tekle, E., and Tjandra, N. (2014) Single color FRET based measurements of conformational changes of proteins resulting from translocation inside cells. Methods 66, 180-187
    • (2014) Methods , vol.66 , pp. 180-187
    • Gahl, R.F.1    Tekle, E.2    Tjandra, N.3
  • 14
    • 0027220591 scopus 로고
    • β-COP is essential for biosynthetic membrane transport from the endoplasmic reticulum to the Golgi complex in vivo
    • Pepperkok, R., Scheel, J., Horstmann, H., Hauri, H. P., Griffiths, G., and Kreis, T. E. (1993) β-COP is essential for biosynthetic membrane transport from the endoplasmic reticulum to the Golgi complex in vivo. Cell 74, 71-82
    • (1993) Cell , vol.74 , pp. 71-82
    • Pepperkok, R.1    Scheel, J.2    Horstmann, H.3    Hauri, H.P.4    Griffiths, G.5    Kreis, T.E.6
  • 15
    • 0242500310 scopus 로고    scopus 로고
    • Inhibition of Bax-induced cytochrome c release from neural cell and brain mitochondria by dibucaine and propranolol
    • Polster, B. M., Basañez, G., Young, M., Suzuki, M., and Fiskum, G. (2003) Inhibition of Bax-induced cytochrome c release from neural cell and brain mitochondria by dibucaine and propranolol. J. Neurosci. 23, 2735-2743
    • (2003) J. Neurosci. , vol.23 , pp. 2735-2743
    • Polster, B.M.1    Basañez, G.2    Young, M.3    Suzuki, M.4    Fiskum, G.5
  • 16
    • 84863205849 scopus 로고    scopus 로고
    • NIH Image to ImageJ: 25 Years of image analysis
    • Schneider, C. A., Rasband, W. S., and Eliceiri, K. W. (2012) NIH Image to ImageJ: 25 years of image analysis. Nat. Methods 9, 671-675
    • (2012) Nat. Methods , vol.9 , pp. 671-675
    • Schneider, C.A.1    Rasband, W.S.2    Eliceiri, K.W.3
  • 17
    • 84873045973 scopus 로고    scopus 로고
    • PINK1 drives Parkin self-association and HECT-like E3 activity upstream of mitochondrial binding
    • Lazarou, M., Narendra, D. P., Jin, S. M., Tekle, E., Banerjee, S., and Youle, R. J. (2013) PINK1 drives Parkin self-association and HECT-like E3 activity upstream of mitochondrial binding. J. Cell Biol. 200, 163-172
    • (2013) J. Cell Biol. , vol.200 , pp. 163-172
    • Lazarou, M.1    Narendra, D.P.2    Jin, S.M.3    Tekle, E.4    Banerjee, S.5    Youle, R.J.6
  • 18
    • 0037331059 scopus 로고    scopus 로고
    • Ultrasensitive investigations of biological systems by fluorescence correlation spectroscopy
    • Haustein, E., and Schwille, P. (2003) Ultrasensitive investigations of biological systems by fluorescence correlation spectroscopy. Methods 29, 153-166
    • (2003) Methods , vol.29 , pp. 153-166
    • Haustein, E.1    Schwille, P.2
  • 19
    • 33644946679 scopus 로고    scopus 로고
    • Peptides corresponding to helices 5 and 6 of Bax can independently form large lipid pores
    • García-Sáez, A. J., Coraiola, M., Serra, M. D., Mingarro, I., Müller, P., and Salgado, J. (2006) Peptides corresponding to helices 5 and 6 of Bax can independently form large lipid pores. FEBS J. 273, 971-981
    • (2006) FEBS J. , vol.273 , pp. 971-981
    • García-Sáez, A.J.1    Coraiola, M.2    Serra, M.D.3    Mingarro, I.4    Müller, P.5    Salgado, J.6
  • 20
    • 22244493864 scopus 로고    scopus 로고
    • Peptides derived from apoptotic Bax and Bid reproduce the poration activity of the parent full-length proteins
    • García-Sáez, A. J., Coraiola, M., Dalla Serra, M., Mingarro, I., Menestrina, G., and Salgado, J. (2005) Peptides derived from apoptotic Bax and Bid reproduce the poration activity of the parent full-length proteins. Biophys. J. 88, 3976-3990
    • (2005) Biophys. J. , vol.88 , pp. 3976-3990
    • García-Sáez, A.J.1    Coraiola, M.2    Dalla Serra, M.3    Mingarro, I.4    Menestrina, G.5    Salgado, J.6
  • 21
    • 0033713002 scopus 로고    scopus 로고
    • Structure of Bax: Coregulation of dimer formation and intracellular localization
    • Suzuki, M., Youle, R. J., and Tjandra, N. (2000) Structure of Bax: coregulation of dimer formation and intracellular localization. Cell 103, 645-654
    • (2000) Cell , vol.103 , pp. 645-654
    • Suzuki, M.1    Youle, R.J.2    Tjandra, N.3
  • 22
    • 0034640133 scopus 로고    scopus 로고
    • Anomalous diffusion of fluorescent probes inside living cell nuclei investigated by spatially-resolved fluorescence correlation spectroscopy
    • Wachsmuth, M., Waldeck, W., and Langowski, J. (2000) Anomalous diffusion of fluorescent probes inside living cell nuclei investigated by spatially-resolved fluorescence correlation spectroscopy. J. Mol. Biol. 298, 677-689
    • (2000) J. Mol. Biol. , vol.298 , pp. 677-689
    • Wachsmuth, M.1    Waldeck, W.2    Langowski, J.3
  • 24
    • 33947409221 scopus 로고    scopus 로고
    • TOM22, a core component of the mitochondria outer membrane protein translocation pore, is a mitochondrial receptor for the proapoptotic protein Bax
    • Bellot, G., Cartron, P.-F., Er, E., Oliver, L., Juin, P., Armstrong, L. C., Bornstein, P., Mihara, K., Manon, S., and Vallette, F. M. (2007) TOM22, a core component of the mitochondria outer membrane protein translocation pore, is a mitochondrial receptor for the proapoptotic protein Bax. Cell Death Differ. 14, 785-794
    • (2007) Cell Death Differ. , vol.14 , pp. 785-794
    • Bellot, G.1    Cartron, P.-F.2    Er, E.3    Oliver, L.4    Juin, P.5    Armstrong, L.C.6    Bornstein, P.7    Mihara, K.8    Manon, S.9    Vallette, F.M.10
  • 26
    • 34548047900 scopus 로고    scopus 로고
    • Crystal structure of ABT-737 complexed with Bcl-xL: Implications for selectivity of antagonists of the Bcl-2 family
    • Lee, E. F., Czabotar, P. E., Smith, B. J., Deshayes, K., Zobel, K., Colman, P. M., and Fairlie, W. D. (2007) Crystal structure of ABT-737 complexed with Bcl-xL: implications for selectivity of antagonists of the Bcl-2 family. Cell Death Differ. 14, 1711-1713
    • (2007) Cell Death Differ. , vol.14 , pp. 1711-1713
    • Lee, E.F.1    Czabotar, P.E.2    Smith, B.J.3    Deshayes, K.4    Zobel, K.5    Colman, P.M.6    Fairlie, W.D.7
  • 27
    • 1542465184 scopus 로고    scopus 로고
    • Interaction with a membrane surface triggers a reversible conformational change in Bax normally associated with induction of apoptosis
    • Yethon, J. A., Epand, R. F., Leber, B., Epand, R. M., and Andrews, D. W. (2003) Interaction with a membrane surface triggers a reversible conformational change in Bax normally associated with induction of apoptosis. J. Biol. Chem. 278, 48935-48941
    • (2003) J. Biol. Chem. , vol.278 , pp. 48935-48941
    • Yethon, J.A.1    Epand, R.F.2    Leber, B.3    Epand, R.M.4    Andrews, D.W.5
  • 28
    • 84858595071 scopus 로고    scopus 로고
    • Cytosolic Bax: Does it require binding proteins to keep its pro-apoptotic activity in check?
    • Vogel, S., Raulf, N., Bregenhorn, S., Biniossek, M. L., Maurer, U., Czabotar, P., and Borner, C. (2012) Cytosolic Bax: does it require binding proteins to keep its pro-apoptotic activity in check? J. Biol. Chem. 287, 9112-9127
    • (2012) J. Biol. Chem. , vol.287 , pp. 9112-9127
    • Vogel, S.1    Raulf, N.2    Bregenhorn, S.3    Biniossek, M.L.4    Maurer, U.5    Czabotar, P.6    Borner, C.7
  • 29
    • 79953192533 scopus 로고    scopus 로고
    • Mutation to Bax beyond the BH3 domain disrupts interactions with pro-survival proteins and promotes apoptosis
    • Czabotar, P. E., Lee, E. F., Thompson, G. V., Wardak, A. Z., Fairlie, W. D., and Colman, P. M. (2011) Mutation to Bax beyond the BH3 domain disrupts interactions with pro-survival proteins and promotes apoptosis. J. Biol. Chem. 286, 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
  • 30
    • 84899462796 scopus 로고    scopus 로고
    • After embedding in membranes antiapoptotic Bcl-XL protein binds both Bcl-2 homology region 3 and helix 1 of proapoptotic Bax protein to inhibit apoptotic mitochondrial permeabilization
    • Ding, J., Mooers, B. H., Zhang, Z., Kale, J., Falcone, D., McNichol, J., Huang, B., Zhang, X. C., Xing, C., Andrews, D. W., and Lin, J. (2014) After embedding in membranes antiapoptotic Bcl-XL protein binds both Bcl-2 homology region 3 and helix 1 of proapoptotic Bax protein to inhibit apoptotic mitochondrial permeabilization. J. Biol. Chem. 289, 11873-11896
    • (2014) J. Biol. Chem. , vol.289 , pp. 11873-11896
    • Ding, J.1    Mooers, B.H.2    Zhang, Z.3    Kale, J.4    Falcone, D.5    McNichol, J.6    Huang, B.7    Zhang, X.C.8    Xing, C.9    Andrews, D.W.10    Lin, J.11
  • 33
    • 84869434589 scopus 로고    scopus 로고
    • Molecular basis for membrane pore formation by Bax protein carboxyl terminus
    • Tatulian, S. A., Garg, P., Nemec, K. N., Chen, B., and Khaled, A. R. (2012) Molecular basis for membrane pore formation by Bax protein carboxyl terminus. Biochemistry 51, 9406-9419
    • (2012) Biochemistry , vol.51 , pp. 9406-9419
    • Tatulian, S.A.1    Garg, P.2    Nemec, K.N.3    Chen, B.4    Khaled, A.R.5
  • 34
    • 21844464054 scopus 로고    scopus 로고
    • Bax forms multispanning monomers that oligomerize to permeabilize membranes during apoptosis
    • Annis, M. G., Soucie, E. L., Dlugosz, P. J., Cruz-Aguado, J. A., Penn, L. Z., Leber, B., and Andrews, D. W. (2005) Bax forms multispanning monomers that oligomerize to permeabilize membranes during apoptosis. EMBO J. 24, 2096-2103
    • (2005) EMBO J. , vol.24 , pp. 2096-2103
    • Annis, M.G.1    Soucie, E.L.2    Dlugosz, P.J.3    Cruz-Aguado, J.A.4    Penn, L.Z.5    Leber, B.6    Andrews, D.W.7
  • 35
    • 84892412571 scopus 로고    scopus 로고
    • Building blocks of the apoptotic pore: How Bax and Bak are activated and oligomerize during apoptosis
    • Westphal, D., Kluck, R. M., and Dewson, G. (2014) Building blocks of the apoptotic pore: how Bax and Bak are activated and oligomerize during apoptosis. Cell Death Differ 21, 196-205
    • (2014) Cell Death Differ , vol.21 , pp. 196-205
    • Westphal, D.1    Kluck, R.M.2    Dewson, G.3
  • 36
    • 82355181105 scopus 로고    scopus 로고
    • BAX unleashed: The biochemical transformation of an inactive cytosolic monomer into a toxic mitochondrial pore
    • Walensky, L. D., and Gavathiotis, E. (2011) BAX unleashed: the biochemical transformation of an inactive cytosolic monomer into a toxic mitochondrial pore. Trends Biochem. Sci. 36, 642-652
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 642-652
    • Walensky, L.D.1    Gavathiotis, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.