메뉴 건너뛰기




Volumn 10, Issue 12, 2003, Pages 1300-1309

Proapoptotic Bid binds to monolysocardiolipin, a new molecular connection between mitochondrial membranes and cell death

Author keywords

Apoptosis; Bid; Cardiolipin; Mitochondria

Indexed keywords

CARDIOLIPIN; PROTEIN BCL 2; PROTEIN BID; RECOMBINANT PROTEIN;

EID: 0348038751     PISSN: 13509047     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.cdd.4401306     Document Type: Article
Times cited : (122)

References (42)
  • 1
    • 0037459081 scopus 로고    scopus 로고
    • Mitochondria: Releasing power for life and unleashing the machineries of death
    • Newmeyer DD and Ferguson-Miller S (2003) Mitochondria:releasing power for life and unleashing the machineries of death. Cell 112: 481-490
    • (2003) Cell , vol.112 , pp. 481-490
    • Newmeyer, D.D.1    Ferguson-Miller, S.2
  • 2
    • 0035890085 scopus 로고    scopus 로고
    • The expanding role of mitochondria in apoptosis
    • Wang X (2001) The expanding role of mitochondria in apoptosis. Genes Dev. 15: 2922-2933
    • (2001) Genes Dev. , vol.15 , pp. 2922-2933
    • Wang, X.1
  • 3
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell death receptors
    • Luo X, Budihardjo I, Zou H, Slaughter C and Wang X (1998) Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell death receptors. Cell 94: 481-490
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 4
    • 0033534446 scopus 로고    scopus 로고
    • Caspase cleaved BID targets mitochondria and is required for cytochrome c release while BCL-XL prevents this release but not tumor necrosis factor death
    • Gross A, Yin XM, Wang K, Wei MC, Jockel J, Milliman C, Erdjument-Bromage H, Tempst P and Korsmeyer SJ (1999) Caspase cleaved BID targets mitochondria and is required for cytochrome c release while BCL-XL prevents this release but not tumor necrosis factor death. J. Biol. Chem. 274: 1156-1163
    • (1999) J. Biol. Chem. , vol.274 , pp. 1156-1163
    • Gross, A.1    Yin, X.M.2    Wang, K.3    Wei, M.C.4    Jockel, J.5    Milliman, C.6    Erdjument-Bromage, H.7    Tempst, P.8    Korsmeyer, S.J.9
  • 5
    • 0036791637 scopus 로고    scopus 로고
    • The roles of Bid
    • Degli Esposti M (2002) The roles of Bid. Apoptosis 7: 433-440
    • (2002) Apoptosis , vol.7 , pp. 433-440
    • Degli Esposti, M.1
  • 7
    • 0034725630 scopus 로고    scopus 로고
    • The destabilisation of lipid membranes induced by the C-terminal fragment of caspase 8-cleaved Bid is inhibited by the N-terminal fragment
    • Kudla G, Montessuit S, Eskes R, Barrier C, Martinou J-C, Ghazi A and Antonsson B (2000) The destabilisation of lipid membranes induced by the C-terminal fragment of caspase 8-cleaved Bid is inhibited by the N-terminal fragment. J. Biol. Chem. 275: 22713-22718
    • (2000) J. Biol. Chem. , vol.275 , pp. 22713-22718
    • Kudla, G.1    Montessuit, S.2    Eskes, R.3    Barrier, C.4    Martinou, J.-C.5    Ghazi, A.6    Antonsson, B.7
  • 8
    • 0034306169 scopus 로고    scopus 로고
    • Cardiolipin provides specificity for targeting of tBid to mitochondria
    • Lutter M, Fang M, Luo X, Nishijima M, Xie X and Wang X (2000) Cardiolipin provides specificity for targeting of tBid to mitochondria. Nat. Cell Biol. 2: 754-756
    • (2000) Nat. Cell Biol. , vol.2 , pp. 754-756
    • Lutter, M.1    Fang, M.2    Luo, X.3    Nishijima, M.4    Xie, X.5    Wang, X.6
  • 9
    • 0034795258 scopus 로고    scopus 로고
    • Bid, a widely expressed pro-apoptotic protein of the Bcl-2 family, displays lipid transfer activity
    • Degli Esposti M, Erler ET, Hickman JA and Dive C (2001) Bid, a widely expressed pro-apoptotic protein of the Bcl-2 family, displays lipid transfer activity. Mol. Cell Biol. 21: 7268-7276
    • (2001) Mol. Cell Biol. , vol.21 , pp. 7268-7276
    • Degli Esposti, M.1    Erler, E.T.2    Hickman, J.A.3    Dive, C.4
  • 12
    • 0037147239 scopus 로고    scopus 로고
    • Bax-type apoptotic proteins porate pure lipid bilayers through a mechanism sensitive to intrinsic monolayer curvature
    • Basanez G, Sharpe JC, Galanis J, Brandt TB, Hardwick JM and Zimmerberg J (2002) Bax-type apoptotic proteins porate pure lipid bilayers through a mechanism sensitive to intrinsic monolayer curvature. J. Biol. Chem. 277: 49360-49365
    • (2002) J. Biol. Chem. , vol.277 , pp. 49360-49365
    • Basanez, G.1    Sharpe, J.C.2    Galanis, J.3    Brandt, T.B.4    Hardwick, J.M.5    Zimmerberg, J.6
  • 15
    • 0034534795 scopus 로고    scopus 로고
    • Posttranslational N-myristoylation of BID as a molecular switch for targeting to mitochondria and apoptosis
    • Zha J, Weiler S, Oh K, Wei MC and Korsmeyer SJ (2000) Posttranslational N-myristoylation of BID as a molecular switch for targeting to mitochondria and apoptosis. Science 290: 1761-1765
    • (2000) Science , vol.290 , pp. 1761-1765
    • Zha, J.1    Weiler, S.2    Oh, K.3    Wei, M.C.4    Korsmeyer, S.J.5
  • 16
    • 0036125351 scopus 로고    scopus 로고
    • Lipids, cardiolipin and apoptosis, a greasy licence to kill
    • Degli Esposti M (2002) Lipids, cardiolipin and apoptosis, a greasy licence to kill. Cell Death Differ. 9: 234-236
    • (2002) Cell Death Differ. , vol.9 , pp. 234-236
    • Degli Esposti, M.1
  • 17
    • 0036863609 scopus 로고    scopus 로고
    • Bax, along with lipid conspirators, allows cytochrome c to escape mitochondria
    • Hardwick JM and Polster BM (2002) Bax, along with lipid conspirators, allows cytochrome c to escape mitochondria. Mol. Cell 10: 963-965
    • (2002) Mol. Cell , vol.10 , pp. 963-965
    • Hardwick, J.M.1    Polster, B.M.2
  • 22
    • 0034193996 scopus 로고    scopus 로고
    • The biosynthesis and functional role of cardiolipin
    • Schlame M, Rua D and Greenberg ML (2000) The biosynthesis and functional role of cardiolipin. Prog. Lip Res. 39: 257-288
    • (2000) Prog. Lip Res. , vol.39 , pp. 257-288
    • Schlame, M.1    Rua, D.2    Greenberg, M.L.3
  • 23
    • 0029831653 scopus 로고    scopus 로고
    • Limited proteolysis of rat phosphatidylinositol transfer protein by trypsin cleaves the C terminus, enhances binding to lipid vesicles, and reduces phospholipid transfer activity
    • Tremblay JM, Helmkamp GM and Yarbrough LR (1996) Limited proteolysis of rat phosphatidylinositol transfer protein by trypsin cleaves the C terminus, enhances binding to lipid vesicles, and reduces phospholipid transfer activity. J. Biol. Chem. 271: 21075-21080
    • (1996) J. Biol. Chem. , vol.271 , pp. 21075-21080
    • Tremblay, J.M.1    Helmkamp, G.M.2    Yarbrough, L.R.3
  • 24
    • 0034817848 scopus 로고    scopus 로고
    • Binding of two mono-acylated lipid monomers by the barley lipid transfer protein, LTP1, as viewed by fluorescence, isothermal titration calorimetry and molecular modelling
    • Douliez JP, Jegou S, Pato C, Molle D, Tran V and Marion D (2001) Binding of two mono-acylated lipid monomers by the barley lipid transfer protein, LTP1, as viewed by fluorescence, isothermal titration calorimetry and molecular modelling. Eur. J. Biochem. 268: 384-388
    • (2001) Eur. J. Biochem. , vol.268 , pp. 384-388
    • Douliez, J.P.1    Jegou, S.2    Pato, C.3    Molle, D.4    Tran, V.5    Marion, D.6
  • 25
    • 0032079544 scopus 로고    scopus 로고
    • Acyl coenzyme A binding protein. Conformational sensitivity to long chain fatty acyl-CoA
    • Frolov A and Schroeder F (1998) Acyl coenzyme A binding protein. Conformational sensitivity to long chain fatty acyl-CoA. J. Biol. Chem. 273: 11049-11055
    • (1998) J. Biol. Chem. , vol.273 , pp. 11049-11055
    • Frolov, A.1    Schroeder, F.2
  • 26
    • 0027089776 scopus 로고
    • A fluorescently labeled intestinal fatty acid protein
    • Richieri GV, Ogata RT and Kleinfeld AM (1992) A fluorescently labeled intestinal fatty acid protein. J. Biol. Chem. 267: 23495-23501
    • (1992) J. Biol. Chem. , vol.267 , pp. 23495-23501
    • Richieri, G.V.1    Ogata, R.T.2    Kleinfeld, A.M.3
  • 27
    • 0028071589 scopus 로고
    • The binding of lysophospholipids to rat liver fatty acid-binding protein
    • Thumser AEA, Voysey JE and Wilton DC (1994) The binding of lysophospholipids to rat liver fatty acid-binding protein. Biochem. J. 301: 801-806
    • (1994) Biochem. J. , vol.301 , pp. 801-806
    • Thumser, A.E.A.1    Voysey, J.E.2    Wilton, D.C.3
  • 28
    • 0028890688 scopus 로고
    • A quantitative electrophoretic migration shift assay for analyzing specific binding of proteins to lipid ligands in vesicles and micelles
    • 1233
    • Arnold M, Ringler P and Brisson A (1995) A quantitative electrophoretic migration shift assay for analyzing specific binding of proteins to lipid ligands in vesicles and micelles. Biochim. Biophys. Acta 1233: 198-204
    • (1995) Biochim. Biophys. Acta , pp. 198-204
    • Arnold, M.1    Ringler, P.2    Brisson, A.3
  • 29
    • 0031007644 scopus 로고    scopus 로고
    • Nonionic detergents induces dimerization among members of the Bcl-2 family
    • Hsu YT and Youle RJ (1997) Nonionic detergents induces dimerization among members of the Bcl-2 family. J. Biol. Chem. 272: 13829-13834
    • (1997) J. Biol. Chem. , vol.272 , pp. 13829-13834
    • Hsu, Y.T.1    Youle, R.J.2
  • 30
    • 0025650402 scopus 로고
    • Lysocardiolipin formation and reacylation in isolated rat liver mitochondria
    • Schlame M and Rustow B (1990) Lysocardiolipin formation and reacylation in isolated rat liver mitochondria. Biochem. J. 272: 589-595
    • (1990) Biochem. J. , vol.272 , pp. 589-595
    • Schlame, M.1    Rustow, B.2
  • 32
    • 0037178881 scopus 로고    scopus 로고
    • Relief of extrinsic pathway inhibition by the Bid-dependent mitochondrial release of Smac in Fas-mediated hepatocyte apoptosis
    • Li S, Zhao Y, He X, Kim TH, Kuharsky DK, Rabinowich H, Chen J, Du C and Yin XM (2002) Relief of extrinsic pathway inhibition by the Bid-dependent mitochondrial release of Smac in Fas-mediated hepatocyte apoptosis. J. Biol. Chem. 277: 26912-26920
    • (2002) J. Biol. Chem. , vol.277 , pp. 26912-26920
    • Li, S.1    Zhao, Y.2    He, X.3    Kim, T.H.4    Kuharsky, D.K.5    Rabinowich, H.6    Chen, J.7    Du, C.8    Yin, X.M.9
  • 33
    • 0037155788 scopus 로고    scopus 로고
    • Cytochrome c release upon Fas receptor activation depends on translocation of full-length bid and the induction of the mitochondrial permeability transition
    • Tafani M, Karpinich NO, Hurster KA, Pastorino JG, Schneider T, Russo MA and Farber JL (2002) Cytochrome c release upon Fas receptor activation depends on translocation of full-length bid and the induction of the mitochondrial permeability transition. J. Biol. Chem. 277: 10073-10082
    • (2002) J. Biol. Chem. , vol.277 , pp. 10073-10082
    • Tafani, M.1    Karpinich, N.O.2    Hurster, K.A.3    Pastorino, J.G.4    Schneider, T.5    Russo, M.A.6    Farber, J.L.7
  • 35
    • 0035819767 scopus 로고    scopus 로고
    • Phospholipids reacylation and palmitoylCoA control tumor necrosis factor-α sensitivity
    • George P, Ardail D, Rey C, Louisot P and Levrat C (2001) Phospholipids reacylation and palmitoylCoA control tumor necrosis factor-α sensitivity. Cytokine 13: 257-263
    • (2001) Cytokine , vol.13 , pp. 257-263
    • George, P.1    Ardail, D.2    Rey, C.3    Louisot, P.4    Levrat, C.5
  • 36
    • 0028790239 scopus 로고
    • Multiple pathways originate at the Fas/APO-1 (CD95) receptor: Sequential involvement of phosphatidycholine-specific phospholipase C and acidic sphingomyelinase in the proagation of the apoptotic signal
    • Cifone MG, Roncaioli P, De Maria R, Camarda G, Santoni A, Ruberti G and Testi R (1995) Multiple pathways originate at the Fas/APO-1 (CD95) receptor: sequential involvement of phosphatidycholine-specific phospholipase C and acidic sphingomyelinase in the proagation of the apoptotic signal. EMBO J. 14: 5859-5868
    • (1995) EMBO J. , vol.14 , pp. 5859-5868
    • Cifone, M.G.1    Roncaioli, P.2    De Maria, R.3    Camarda, G.4    Santoni, A.5    Ruberti, G.6    Testi, R.7
  • 37
    • 0023657091 scopus 로고
    • Inhibition of mitochondrial phospholipase A2 by mono- and dilysocardiolipin
    • Reers M and Pfeiffer DR (1987) Inhibition of mitochondrial phospholipase A2 by mono- and dilysocardiolipin. Biochemistry 26: 8038-8041
    • (1987) Biochemistry , vol.26 , pp. 8038-8041
    • Reers, M.1    Pfeiffer, D.R.2
  • 38
    • 0032577596 scopus 로고    scopus 로고
    • Fas-induced arachidonic acid release is mediated by Ca2+-independent phospholipase A2 but not cytosolic phospholipase A2, which undergoes proteolytic inactivation
    • Atsumi G, Tajima M, Hadano A, Nakatani Y, Murakami M and Kudo I (1998) Fas-induced arachidonic acid release is mediated by Ca2+-independent phospholipase A2 but not cytosolic phospholipase A2, which undergoes proteolytic inactivation. J. Biol. Chem. 273: 13870-13877
    • (1998) J. Biol. Chem. , vol.273 , pp. 13870-13877
    • Atsumi, G.1    Tajima, M.2    Hadano, A.3    Nakatani, Y.4    Murakami, M.5    Kudo, I.6
  • 40
    • 0035865416 scopus 로고    scopus 로고
    • Detection of individual phospholipids in lipid mixtures by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Petkovic M, Schiller J, Muller M, Bernard S, Reichl S, Arnold K and Arnhold J (2001) Detection of individual phospholipids in lipid mixtures by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Anal. Biochem. 289:202-216
    • (2001) Anal. Biochem. , vol.289 , pp. 202-216
    • Petkovic, M.1    Schiller, J.2    Muller, M.3    Bernard, S.4    Reichl, S.5    Arnold, K.6    Arnhold, J.7
  • 41
    • 0032762951 scopus 로고    scopus 로고
    • Intramolecularly quenched BODIPY-labeled phospolipid analogs in phospholipase A2 and platelet-activating factor acetylhydrolase assays and in vivo fluorescence imaging
    • Hendrickson HS, Hendrickson EK, Johnson ID and Farber SA (1999) Intramolecularly quenched BODIPY-labeled phospolipid analogs in phospholipase A2 and platelet-activating factor acetylhydrolase assays and in vivo fluorescence imaging. Anal. Biochem. 276: 27-35
    • (1999) Anal. Biochem. , vol.276 , pp. 27-35
    • Hendrickson, H.S.1    Hendrickson, E.K.2    Johnson, I.D.3    Farber, S.A.4
  • 42
    • 0024286579 scopus 로고
    • Quenching of the intrinsic tryptophan fluorescence of the mitochondrial ubiquinol-cytochrome-c reductase by the binding of ubiquinone
    • Samworth CM, Degli Esposti M and Lenaz G (1988) Quenching of the intrinsic tryptophan fluorescence of the mitochondrial ubiquinol-cytochrome-c reductase by the binding of ubiquinone. Eur. J. Biochem. 171: 81-86
    • (1988) Eur. J. Biochem. , vol.171 , pp. 81-86
    • Samworth, C.M.1    Degli Esposti, M.2    Lenaz, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.