메뉴 건너뛰기




Volumn 586, Issue 2, 2012, Pages 116-121

The cytosolic domain of human Tom22 modulates human Bax mitochondrial translocation and conformation in yeast

Author keywords

Apoptosis; Bax translocation; TOM; Yeast mitochondria

Indexed keywords

PROTEIN BAX; PROTEIN TOM22; RECEPTOR; RECEPTOR SUBUNIT; UNCLASSIFIED DRUG;

EID: 84855781215     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2011.12.003     Document Type: Article
Times cited : (16)

References (30)
  • 1
    • 0036716281 scopus 로고    scopus 로고
    • The BCL2 family: Regulators of the cellular life-or-death switch
    • DOI 10.1038/nrc883
    • S. Cory, and J.M. Adams The Bcl2 family: regulators of the cellular life-or-death switch Nat. Rev. Cancer 2 2002 647 656 (Pubitemid 37328916)
    • (2002) Nature Reviews Cancer , vol.2 , Issue.9 , pp. 647-656
    • Cory, S.1    Adams, J.M.2
  • 3
    • 79960845529 scopus 로고    scopus 로고
    • Bax: Addressed to kill
    • T.T. Renault, and S. Manon Bax: Addressed to kill Biochimie 93 2011 1379 1391
    • (2011) Biochimie , vol.93 , pp. 1379-1391
    • Renault, T.T.1    Manon, S.2
  • 5
    • 67650741483 scopus 로고    scopus 로고
    • Mitochondrial targeting of tBid/Bax: A role for the TOM complex?
    • M. Ott, E. Norberg, B. Zhivotovsky, and S. Orrenius Mitochondrial targeting of tBid/Bax: a role for the TOM complex? Cell Death Differ. 16 2009 1075 1082
    • (2009) Cell Death Differ. , vol.16 , pp. 1075-1082
    • Ott, M.1    Norberg, E.2    Zhivotovsky, B.3    Orrenius, S.4
  • 6
    • 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
    • DOI 10.1038/sj.cdd.4402055, PII 4402055
    • G. Bellot, P.F. Cartron, E. Er, L. Oliver, P. Juin, L.C. Armstrong, P. Bornstein, K. Mihara, S. Manon, and F.M. Vallette 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 2007 785 794 (Pubitemid 46444516)
    • (2007) Cell Death and Differentiation , vol.14 , Issue.4 , 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
  • 11
    • 0037070160 scopus 로고    scopus 로고
    • Involvement of the N-terminus of Bax in its intracellular localization and function
    • DOI 10.1016/S0014-5793(02)02227-5, PII S0014579302022275
    • P.F. Cartron, C. Moreau, L. Oliver, E. Mayat, K. Meflah, and F.M. Vallette Involvement of the N-terminus of Bax in its intracellular localization and function FEBS Lett. 512 2002 95 100 (Pubitemid 34164458)
    • (2002) FEBS Letters , vol.512 , Issue.1-3 , pp. 95-100
    • Cartron, P.-F.1    Moreau, C.2    Oliver, L.3    Mayat, E.4    Meflah, K.5    Vallette, F.M.6
  • 13
    • 1642565065 scopus 로고    scopus 로고
    • The p18 Truncated Form of Bax Behaves Like a Bcl-2 Homology Domain 3-only Protein
    • DOI 10.1074/jbc.M311922200
    • P.F. Cartron, L. Oliver, P. Juin, K. Meflah, and F.M. Vallette The p18 truncated form of Bax behaves like a Bcl-2 homology domain 3-only protein J. Biol. Chem. 279 2004 11503 11512 (Pubitemid 38401650)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.12 , pp. 11503-11512
    • Cartron, P.-F.1    Oliver, L.2    Juin, P.3    Meflah, K.4    Vallette, F.M.5
  • 14
    • 47249105254 scopus 로고    scopus 로고
    • Bax targeting to mitochondria occurs via both tail anchor-dependent and -independent mechanisms
    • DOI 10.1038/cdd.2008.39, PII CDD200839
    • A.J. Valentijn, J.P. Upton, N. Bates, and A.P. Gilmore Bax targeting to mitochondria occurs via both tail anchor-dependent and -independent mechanisms Cell Death Differ. 15 2008 1243 1254 (Pubitemid 351984754)
    • (2008) Cell Death and Differentiation , vol.15 , Issue.8 , pp. 1243-1254
    • Valentijn, A.J.1    Upton, J.-P.2    Bates, N.3    Gilmore, A.P.4
  • 15
    • 65249133454 scopus 로고    scopus 로고
    • TOM-independent complex formation of Bax and Bak in mammalian mitochondria during TNFalpha-induced apoptosis
    • K. Ross, T. Rudel, and V. Kozjak-Pavlovic TOM-independent complex formation of Bax and Bak in mammalian mitochondria during TNFalpha-induced apoptosis Cell Death Differ. 16 2009 697 707
    • (2009) Cell Death Differ. , vol.16 , pp. 697-707
    • Ross, K.1    Rudel, T.2    Kozjak-Pavlovic, V.3
  • 16
    • 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
  • 17
    • 10644224222 scopus 로고    scopus 로고
    • L
    • DOI 10.1074/jbc.M408373200
    • H. Arokium, N. Camougrand, F.M. Vallette, and S. Manon Studies of the interaction of substituted mutants of BAX with yeast mitochondria reveal that the C-terminal hydrophobic alpha-helix is a second ART sequence and plays a role in the interaction with anti-apoptotic BCL-xL J. Biol. Chem. 279 2004 52566 52573 (Pubitemid 39656633)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.50 , pp. 52566-52573
    • Arokium, H.1    Camougrand, N.2    Vallette, F.M.3    Manon, S.4
  • 18
    • 77955282104 scopus 로고    scopus 로고
    • Upregulation of Bcl2 inhibits apoptosis-driven BAX insertion but favors BAX relocalization in mitochondria
    • O. Teijido, and L. Dejean Upregulation of Bcl2 inhibits apoptosis-driven BAX insertion but favors BAX relocalization in mitochondria FEBS Lett. 584 2010 3305 3310
    • (2010) FEBS Lett. , vol.584 , pp. 3305-3310
    • Teijido, O.1    Dejean, L.2
  • 22
    • 0032527780 scopus 로고    scopus 로고
    • Interaction of mitochondrial targeting signals with acidic receptor domains along the protein import pathway: Evidence for the 'acid chain' hypothesis
    • DOI 10.1093/emboj/17.14.3886
    • T. Komiya, S. Rospert, C. Koehler, R. Looser, G. Schatz, and K. Mihara Interaction of mitochondrial targeting signals with acidic receptor domains along the protein import pathway: evidence for the 'acid chain' hypothesis EMBO J. 17 1998 3886 3898 (Pubitemid 28333975)
    • (1998) EMBO Journal , vol.17 , Issue.14 , pp. 3886-3898
    • Komiya, T.1    Rospert, S.2    Koehler, C.3    Looser, R.4    Schatz, G.5    Mihara, K.6
  • 23
    • 0033834702 scopus 로고    scopus 로고
    • Identification and functional analysis of human Tom22 for protein import into mitochondria
    • M. Yano, N. Hoogenraad, K. Terada, and M. Mori Identification and functional analysis of human Tom22 for protein import into mitochondria Mol. Cell. Biol. 20 2000 7205 7213
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7205-7213
    • Yano, M.1    Hoogenraad, N.2    Terada, K.3    Mori, M.4
  • 25
  • 26
    • 58949102766 scopus 로고    scopus 로고
    • The mitochondrial TOM complex modulates bax-induced apoptosis in Drosophila
    • J. Colin, J. Garibal, B. Mignotte, and I. Guénal The mitochondrial TOM complex modulates bax-induced apoptosis in Drosophila Biochem. Biophys. Res. Commun. 379 2009 939 943
    • (2009) Biochem. Biophys. Res. Commun. , vol.379 , pp. 939-943
    • Colin, J.1    Garibal, J.2    Mignotte, B.3    Guénal, I.4
  • 28
    • 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
  • 29
    • 0036977273 scopus 로고    scopus 로고
    • Bcl-2 and porin follow different pathways of TOM-dependent insertion into the mitochondrial outer membrane
    • DOI 10.1016/S0022-2836(02)00995-6
    • C. Motz, H. Martin, T. Krimmer, and J. Rassow Bcl-2 and porin follow different pathways of TOM-dependent insertion into the mitochondrial outer membrane J. Mol. Biol. 323 2002 729 738 (Pubitemid 36160226)
    • (2002) Journal of Molecular Biology , vol.323 , Issue.4 , pp. 729-738
    • Motz, C.1    Martin, H.2    Krimmer, T.3    Rassow, J.4
  • 30
    • 42949139525 scopus 로고    scopus 로고
    • Tom20 and Tom22 share the common signal recognition pathway in mitochondrial protein import
    • K. Yamano, Y. Yatsukawa, M. Esaki, A.E. Hobbs, R.E. Jensen, and T. Endo Tom20 and Tom22 share the common signal recognition pathway in mitochondrial protein import J. Biol. Chem. 283 2008 3799 3807
    • (2008) J. Biol. Chem. , vol.283 , pp. 3799-3807
    • Yamano, K.1    Yatsukawa, Y.2    Esaki, M.3    Hobbs, A.E.4    Jensen, R.E.5    Endo, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.