메뉴 건너뛰기




Volumn 15, Issue 8, 2008, Pages 1243-1254

Bax targeting to mitochondria occurs via both tail anchor-dependent and -independent mechanisms

Author keywords

[No Author keywords available]

Indexed keywords

MITOCHONDRIAL PROTEIN; MUTANT PROTEIN; OUTER MEMBRANE PROTEIN; PROTEIN BAK; PROTEIN BAX;

EID: 47249105254     PISSN: 13509047     EISSN: 14765403     Source Type: Journal    
DOI: 10.1038/cdd.2008.39     Document Type: Article
Times cited : (42)

References (40)
  • 1
    • 0036716281 scopus 로고    scopus 로고
    • The Bcl2 family: Regulators of the cellular life-or-death switch
    • Cory S, Adams JM. The Bcl2 family: Regulators of the cellular life-or-death switch. Nat Rev Cancer 2002; 2: 647-656.
    • (2002) Nat Rev Cancer , vol.2 , pp. 647-656
    • Cory, S.1    Adams, J.M.2
  • 2
    • 0035957653 scopus 로고    scopus 로고
    • Proapoptofic BAX and BAK: A requisite gateway to mitochondrial dysfunction and death
    • Wei MC, Zong WX, Chang EH, Lindsten T, Panoutsakopoulou V, Ross AJ et al. Proapoptofic BAX and BAK: A requisite gateway to mitochondrial dysfunction and death. Science 2001; 292: 727-730.
    • (2001) Science , vol.292 , pp. 727-730
    • Wei, M.C.1    Zong, W.X.2    Chang, E.H.3    Lindsten, T.4    Panoutsakopoulou, V.5    Ross, A.J.6
  • 3
    • 0034678367 scopus 로고    scopus 로고
    • Integrin-mediated survival signals regulate the apoptotic function of Bax through its conformation and subcellular localization
    • Gilmore AP, Metcalfe AM, Romer LH, Streuli CH. Integrin-mediated survival signals regulate the apoptotic function of Bax through its conformation and subcellular localization. J Cell Biol 2000; 149: 431-445.
    • (2000) J Cell Biol , vol.149 , pp. 431-445
    • Gilmore, A.P.1    Metcalfe, A.M.2    Romer, L.H.3    Streuli, C.H.4
  • 5
    • 0035853811 scopus 로고    scopus 로고
    • Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells
    • Antonsson B, Montessuit S, Sanchez B, Martinou JC. Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells. J Biol Chem 2001; 276: 11615-11623.
    • (2001) J Biol Chem , vol.276 , pp. 11615-11623
    • Antonsson, B.1    Montessuit, S.2    Sanchez, B.3    Martinou, J.C.4
  • 6
    • 0033535350 scopus 로고    scopus 로고
    • Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis
    • Desagher S, Osen Sand A, Nichols A, Eskes R, Montessuit S, Lauper S et al. Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis. J Cell Biol 1999; 144: 891-901.
    • (1999) J Cell Biol , vol.144 , pp. 891-901
    • Desagher, S.1    Osen Sand, A.2    Nichols, A.3    Eskes, R.4    Montessuit, S.5    Lauper, S.6
  • 7
    • 0033981577 scopus 로고    scopus 로고
    • Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane
    • Eskes R, Desagher S, Antonsson B, Martinou JC. Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane. Mol Cel Biol 2000; 20: 929-935.
    • (2000) Mol Cel Biol , vol.20 , pp. 929-935
    • Eskes, R.1    Desagher, S.2    Antonsson, B.3    Martinou, J.C.4
  • 8
    • 0030963602 scopus 로고    scopus 로고
    • Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis
    • Hsu YT, Wolter KG, Youle RJ. Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis. Proc Natl Acad Sci USA 1997; 94 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
  • 11
    • 0035344460 scopus 로고    scopus 로고
    • Versatility of the mitochondrial protein import machinery
    • Planner N, Geissler A. Versatility of the mitochondrial protein import machinery. Nat Rev Mol Cell Biol 2001; 2: 339-349.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 339-349
    • Planner, N.1    Geissler, A.2
  • 12
    • 34547937485 scopus 로고    scopus 로고
    • How tails guide tail-anchored proteins to their destinations
    • Borgese N, Brambillasca S, Colombo S. How tails guide tail-anchored proteins to their destinations. Curr Opin Cell Biol 2007; 19 368-375.
    • (2007) Curr Opin Cell Biol , vol.19 , pp. 368-375
    • Borgese, N.1    Brambillasca, S.2    Colombo, S.3
  • 13
    • 0036000002 scopus 로고    scopus 로고
    • Characterization of signal that directs C-tail-anchored proteins to mammalian mitochondrial outer membrane
    • Horie C, Suzuki H, Sakaguchi M, Where K. Characterization of signal that directs C-tail-anchored proteins to mammalian mitochondrial outer membrane. Mol Biol Cell 2002; 13: 1615-1625.
    • (2002) Mol Biol Cell , vol.13 , pp. 1615-1625
    • Horie, C.1    Suzuki, H.2    Sakaguchi, M.3    Where, K.4
  • 14
    • 0037421190 scopus 로고    scopus 로고
    • Characterization of the signal that directs Bcl-x(L), but not Bcl-2, to the mitochondrial outer membrane
    • Kaufmann T, Schlipf S, Sanz J, Neubert K, Stain R, Bomer C. Characterization of the signal that directs Bcl-x(L), but not Bcl-2, to the mitochondrial outer membrane. J Cell Biol 2003; 160: 53-64.
    • (2003) J Cell Biol , vol.160 , pp. 53-64
    • Kaufmann, T.1    Schlipf, S.2    Sanz, J.3    Neubert, K.4    Stain, R.5    Bomer, C.6
  • 15
    • 1442359881 scopus 로고    scopus 로고
    • Bcl-2 family members: Intracellular targeting, membrane-insertion, and changes in subcellular localization
    • Schinzel A, Kaufmann T, Bomer C. Bcl-2 family members: Intracellular targeting, membrane-insertion, and changes in subcellular localization. Biochim Biophys Acta 2004; 1644: 95-105.
    • (2004) Biochim Biophys Acta , vol.1644 , pp. 95-105
    • Schinzel, A.1    Kaufmann, T.2    Bomer, C.3
  • 16
    • 0027166048 scopus 로고
    • Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death
    • Oltvai ZN, Milliman CL, Korsmeyer SJ. Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death. Cell 1993; 74: 609-619.
    • (1993) Cell , vol.74 , pp. 609-619
    • Oltvai, Z.N.1    Milliman, C.L.2    Korsmeyer, S.J.3
  • 17
    • 15444364107 scopus 로고    scopus 로고
    • Distinct domains control the addressing and the insertion of Bax into mitochondria
    • Cartron PF, Arokium H, Oliver L, Meflah K, Manon S, Vallette FM. Distinct domains control the addressing and the insertion of Bax into mitochondria. J Biol Chem 2005; 280: 10587-10598.
    • (2005) J Biol Chem , vol.280 , pp. 10587-10598
    • Cartron, P.F.1    Arokium, H.2    Oliver, L.3    Meflah, K.4    Manon, S.5    Vallette, F.M.6
  • 19
    • 0037070160 scopus 로고    scopus 로고
    • Involvement of the N-terminus of Bax in its intracellular localization and function
    • Cartron PF, Moreau C, Oliver L, Mayat E, Meflah K, Vallette FM. Involvement of the N-terminus of Bax in its intracellular localization and function. FEBS Lett 2002; 512: 95-100.
    • (2002) FEBS Lett , vol.512 , pp. 95-100
    • Cartron, P.F.1    Moreau, C.2    Oliver, L.3    Mayat, E.4    Meflah, K.5    Vallette, F.M.6
  • 21
    • 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 PF, Er E, Oliver L, Juin P, Armstrong LC et al. TOM22, a core component of the mitochondria outer membrane protein translocation pore, is a mitochondrial receptor for the proapoptotic protein Bax. Cell Death Differ 2007; 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
  • 22
    • 0033522391 scopus 로고    scopus 로고
    • Conformation of the Bax C-terminus regulates subcellular location and cell death
    • Nechushtan A, Smith CL, Hsu YT, Youle RJ. Conformation of the Bax C-terminus regulates subcellular location and cell death. EMBO J 1999; 18: 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
  • 24
    • 34247354978 scopus 로고    scopus 로고
    • The N-terminal conformation of Bax regulates cell commitment to apoptosis
    • Upton JP, Valentijn AJ, Zhang L, Gilmore AP. The N-terminal conformation of Bax regulates cell commitment to apoptosis. Cell Death Differ 2007; 14: 932-942.
    • (2007) Cell Death Differ , vol.14 , pp. 932-942
    • Upton, J.P.1    Valentijn, A.J.2    Zhang, L.3    Gilmore, A.P.4
  • 27
    • 0028234557 scopus 로고
    • Mitochondrial Mas70p signal anchor sequence. Mutations in the transmembrane domain that disrupt dimerization but not targeting or membrane insertion
    • Millar DG, Shore GC. Mitochondrial Mas70p signal anchor sequence. Mutations in the transmembrane domain that disrupt dimerization but not targeting or membrane insertion. J Biol Chem 1994; 269: 12229-12232.
    • (1994) J Biol Chem , vol.269 , pp. 12229-12232
    • Millar, D.G.1    Shore, G.C.2
  • 28
    • 2942625430 scopus 로고    scopus 로고
    • Bcl-x(L) sequesters its C-terminal membrane anchor in soluble, cytosolic homodimers
    • Jeong SY, Gaume B, Lee YJ, Hsu YT, Ryu SW, Yoon SH et al. Bcl-x(L) sequesters its C-terminal membrane anchor in soluble, cytosolic homodimers. EMBO J 2004; 23: 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
  • 29
    • 0035844867 scopus 로고    scopus 로고
    • Bax and Bak coalesce into novel mitochondria-associated clusters during apoptosis
    • Nechushtan A, Smith CL, Lamensdorf I, Yoon SH, Youle RJ. Bax and Bak coalesce into novel mitochondria-associated clusters during apoptosis. J Cell Biol 2001; 153: 1265-1276.
    • (2001) J Cell Biol , vol.153 , pp. 1265-1276
    • Nechushtan, A.1    Smith, C.L.2    Lamensdorf, I.3    Yoon, S.H.4    Youle, R.J.5
  • 30
    • 0042090307 scopus 로고    scopus 로고
    • BCL-2 selectively interacts with the BID-induced open conformer of BAK, inhibiting BAK auto-oligomerization
    • Ruffolo SC, Shore GC. BCL-2 selectively interacts with the BID-induced open conformer of BAK, inhibiting BAK auto-oligomerization. J Biol Chem 2003; 278: 25039-25045.
    • (2003) J Biol Chem , vol.278 , pp. 25039-25045
    • Ruffolo, S.C.1    Shore, G.C.2
  • 31
    • 33744953583 scopus 로고    scopus 로고
    • Auto-aclivation of the apoptosis protein Bax increases mitochondrial membrane permeability and is inhibited by Bcl-2
    • Tan C, Dlugosz PJ, Peng J, Zhang Z, Lapolla SM, Plafker SM et al. Auto-aclivation of the apoptosis protein Bax increases mitochondrial membrane permeability and is inhibited by Bcl-2. J Biol Chem 2006; 281: 14764-14775.
    • (2006) J Biol Chem , vol.281 , pp. 14764-14775
    • Tan, C.1    Dlugosz, P.J.2    Peng, J.3    Zhang, Z.4    Lapolla, S.M.5    Plafker, S.M.6
  • 32
    • 34250183921 scopus 로고    scopus 로고
    • Post-translational integration of tail-anchored proteins is facilitated by defined molecular chaperones
    • Abell BM, Rabu C, Leznicki P, Young JC, High S. Post-translational integration of tail-anchored proteins is facilitated by defined molecular chaperones. J Cell Sci 2007; 120: 1743-1751.
    • (2007) J Cell Sci , vol.120 , pp. 1743-1751
    • Abell, B.M.1    Rabu, C.2    Leznicki, P.3    Young, J.C.4    High, S.5
  • 33
    • 33947218544 scopus 로고    scopus 로고
    • Identification of a targeting factor for posttranslational membrane protein insertion into the ER
    • Stefanovic S, Hegde RS. Identification of a targeting factor for posttranslational membrane protein insertion into the ER. Cell 2007; 128: 1147-1159.
    • (2007) Cell , vol.128 , pp. 1147-1159
    • Stefanovic, S.1    Hegde, R.S.2
  • 34
    • 0033713002 scopus 로고    scopus 로고
    • Structure of Bax: Coregulation of dimer formation and intracellular localization
    • Suzuki M, Youle RJ, Tjandra N. Structure of Bax: Coregulation of dimer formation and intracellular localization. Cell 2000; 103: 645-654.
    • (2000) Cell , vol.103 , pp. 645-654
    • Suzuki, M.1    Youle, R.J.2    Tjandra, N.3
  • 35
    • 0036850312 scopus 로고    scopus 로고
    • Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane
    • Kuwana T, Mackey MR, Perkins G, Ellisman MH, Latterich M, Schneiter R et al. Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane. Cell 2002; 111: 331-342.
    • (2002) Cell , vol.111 , pp. 331-342
    • Kuwana, T.1    Mackey, M.R.2    Perkins, G.3    Ellisman, M.H.4    Latterich, M.5    Schneiter, R.6
  • 36
    • 0037115740 scopus 로고    scopus 로고
    • Bax oligomerization in mitochondrial membranes requires tBid (caspase-8-cleaved Bid) and a mitochondrial protein
    • Roucou X, Montessuit S, Antonsson B, Martinou JC. Bax oligomerization in mitochondrial membranes requires tBid (caspase-8-cleaved Bid) and a mitochondrial protein. Biochem J 2002; 368: 915-921.
    • (2002) Biochem J , vol.368 , pp. 915-921
    • Roucou, X.1    Montessuit, S.2    Antonsson, B.3    Martinou, J.C.4
  • 37
    • 34948850958 scopus 로고    scopus 로고
    • The mitochondrial TOM complex is required for tBid/Bax-induced cytochrome c release
    • Ott M, Norberg E, Walter KM, Schreiner P, Kemper C, Rapaport D et al The mitochondrial TOM complex is required for tBid/Bax-induced cytochrome c release. J Biol Chem 2007; 282: 27633-27639.
    • (2007) J Biol Chem , vol.282 , pp. 27633-27639
    • Ott, M.1    Norberg, E.2    Walter, K.M.3    Schreiner, P.4    Kemper, C.5    Rapaport, D.6
  • 38
    • 33947321082 scopus 로고    scopus 로고
    • Preprotein transport machineries of yeast mitochondrial outer membrane are not required for Bax-induced release of intermembrane space proteins
    • Sanjuan Szldarz LK, Kozjak-Pavlovic V, Vogtle FN, Chacinska A, Milenkovic D, Vogel S et al. Preprotein transport machineries of yeast mitochondrial outer membrane are not required for Bax-induced release of intermembrane space proteins. J Mol Biol 2007; 368 44-54.
    • (2007) J Mol Biol , vol.368 , pp. 44-54
    • Sanjuan Szldarz, L.K.1    Kozjak-Pavlovic, V.2    Vogtle, F.N.3    Chacinska, A.4    Milenkovic, D.5    Vogel, S.6
  • 39
    • 33845685298 scopus 로고    scopus 로고
    • Cytosolic factor- and TOM-independent import of C-tail-anchored mitochondrial outer membrane proteins
    • Setoguchi K, Otera H, Mihara K. Cytosolic factor- and TOM-independent import of C-tail-anchored mitochondrial outer membrane proteins. EMBO J 2006; 25: 5635-5647.
    • (2006) EMBO J , vol.25 , pp. 5635-5647
    • Setoguchi, K.1    Otera, H.2    Mihara, K.3
  • 40
    • 0036668515 scopus 로고    scopus 로고
    • High throughput two-dimensional blue-native electrophoresis: A tool for functional proteomics of mitochondria and signaling complexes
    • Brookes PS, Pinner A, Ramachandran A, Coward L, Barnes S, Kim H et al High throughput two-dimensional blue-native electrophoresis: A tool for functional proteomics of mitochondria and signaling complexes. Proteomics 2002; 2: 969-977.
    • (2002) Proteomics , vol.2 , pp. 969-977
    • Brookes, P.S.1    Pinner, A.2    Ramachandran, A.3    Coward, L.4    Barnes, S.5    Kim, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.