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Volumn 16, Issue 7, 2015, Pages 813-823

Structural basis of intramitochondrial phosphatidic acid transport mediated by Ups1-Mdm35 complex

Author keywords

cardiolipin synthesis; lipid transfer protein; mitochondrial morphology; phosphatidic acid transport

Indexed keywords

PHOSPHATIDIC ACID; PROTEIN; PROTEIN MDM35; PROTEIN UPS1; UNCLASSIFIED DRUG; CARDIOLIPIN; MDM35 PROTEIN, S CEREVISIAE; MITOCHONDRIAL PROTEIN; PHOSPHOLIPID; SACCHAROMYCES CEREVISIAE PROTEIN; UPS1 PROTEIN, S CEREVISIAE;

EID: 84934824355     PISSN: 1469221X     EISSN: 14693178     Source Type: Journal    
DOI: 10.15252/embr.201540137     Document Type: Article
Times cited : (47)

References (41)
  • 1
    • 14644393694 scopus 로고    scopus 로고
    • Lipid traffic: Floppy drives and a superhighway
    • Holthuis JC, Levine TP, (2005) Lipid traffic: floppy drives and a superhighway. Nat Rev Mol Cell Biol 6: 209-220
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 209-220
    • Holthuis, J.C.1    Levine, T.P.2
  • 3
    • 77957134067 scopus 로고    scopus 로고
    • Non-vesicular lipid transport by lipid-transfer proteins and beyond
    • Lev S, (2010) Non-vesicular lipid transport by lipid-transfer proteins and beyond. Nat Rev Mol Cell Biol 11: 739-750
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 739-750
    • Lev, S.1
  • 4
    • 78649967779 scopus 로고    scopus 로고
    • Lipid trafficking sans vesicles: Where, why, how?
    • Prinz WA, (2010) Lipid trafficking sans vesicles: where, why, how? Cell 143: 870-874
    • (2010) Cell , vol.143 , pp. 870-874
    • Prinz, W.A.1
  • 5
    • 33750264683 scopus 로고    scopus 로고
    • Phosphatidylinositol transfer proteins and cellular nanoreactors for lipid signaling
    • Ile KE, Schaaf G, Bankaitis VA, (2006) Phosphatidylinositol transfer proteins and cellular nanoreactors for lipid signaling. Nat Chem Biol 2: 576-583
    • (2006) Nat Chem Biol , vol.2 , pp. 576-583
    • Ile, K.E.1    Schaaf, G.2    Bankaitis, V.A.3
  • 6
    • 24344455560 scopus 로고    scopus 로고
    • Structural mechanism for sterol sensing and transport by OSBP-related proteins
    • Im YJ, Raychaudhuri S, Prinz WA, Hurley JH, (2005) Structural mechanism for sterol sensing and transport by OSBP-related proteins. Nature 437: 154-158
    • (2005) Nature , vol.437 , pp. 154-158
    • Im, Y.J.1    Raychaudhuri, S.2    Prinz, W.A.3    Hurley, J.H.4
  • 8
    • 33645727511 scopus 로고    scopus 로고
    • Nonvesicular sterol movement from plasma membrane to ER requires oxysterol-binding protein-related proteins and phosphoinositides
    • Raychaudhuri S, Im YJ, Hurley JH, Prinz WA, (2006) Nonvesicular sterol movement from plasma membrane to ER requires oxysterol-binding protein-related proteins and phosphoinositides. J Cell Biol 173: 107-119
    • (2006) J Cell Biol , vol.173 , pp. 107-119
    • Raychaudhuri, S.1    Im, Y.J.2    Hurley, J.H.3    Prinz, W.A.4
  • 11
    • 78651287877 scopus 로고    scopus 로고
    • Making heads or tails of phospholipids in mitochondria
    • Osman C, Voelker DR, Langer T, (2011) Making heads or tails of phospholipids in mitochondria. J Cell Biol 192: 7-16
    • (2011) J Cell Biol , vol.192 , pp. 7-16
    • Osman, C.1    Voelker, D.R.2    Langer, T.3
  • 13
    • 77956391459 scopus 로고    scopus 로고
    • Regulation of mitochondrial phospholipids by Ups1/PRELI-like proteins depends on proteolysis and Mdm35
    • Potting C, Wilmes C, Engmann T, Osman C, Langer T, (2010) Regulation of mitochondrial phospholipids by Ups1/PRELI-like proteins depends on proteolysis and Mdm35. EMBO J 29: 2888-2898
    • (2010) EMBO J , vol.29 , pp. 2888-2898
    • Potting, C.1    Wilmes, C.2    Engmann, T.3    Osman, C.4    Langer, T.5
  • 14
    • 18644373097 scopus 로고    scopus 로고
    • A novel family of mitochondrial proteins is represented by the Drosophila genes slmo, preli-like and real-time
    • Dee CT, Moffat KG, (2005) A novel family of mitochondrial proteins is represented by the Drosophila genes slmo, preli-like and real-time. Dev Genes Evol 215: 248-254
    • (2005) Dev Genes Evol , vol.215 , pp. 248-254
    • Dee, C.T.1    Moffat, K.G.2
  • 15
    • 33747422544 scopus 로고    scopus 로고
    • Ups1p, a conserved intermembrane space protein, regulates mitochondrial shape and alternative topogenesis of Mgm1p
    • Sesaki H, Dunn CD, Iijima M, Shepard KA, Yaffe MP, Machamer CE, Jensen RE, (2006) Ups1p, a conserved intermembrane space protein, regulates mitochondrial shape and alternative topogenesis of Mgm1p. J Cell Biol 173: 651-658
    • (2006) J Cell Biol , vol.173 , pp. 651-658
    • Sesaki, H.1    Dunn, C.D.2    Iijima, M.3    Shepard, K.A.4    Yaffe, M.P.5    MacHamer, C.E.6    Jensen, R.E.7
  • 16
    • 67449138848 scopus 로고    scopus 로고
    • Ups1p and Ups2p antagonistically regulate cardiolipin metabolism in mitochondria
    • Tamura Y, Endo T, Iijima M, Sesaki H, (2009) Ups1p and Ups2p antagonistically regulate cardiolipin metabolism in mitochondria. J Cell Biol 185: 1029-1045
    • (2009) J Cell Biol , vol.185 , pp. 1029-1045
    • Tamura, Y.1    Endo, T.2    Iijima, M.3    Sesaki, H.4
  • 17
    • 77956378766 scopus 로고    scopus 로고
    • Mdm35p imports Ups proteins into the mitochondrial intermembrane space by functional complex formation
    • Tamura Y, Iijima M, Sesaki H, (2010) Mdm35p imports Ups proteins into the mitochondrial intermembrane space by functional complex formation. EMBO J 29: 2875-2887
    • (2010) EMBO J , vol.29 , pp. 2875-2887
    • Tamura, Y.1    Iijima, M.2    Sesaki, H.3
  • 18
    • 84856853161 scopus 로고    scopus 로고
    • Mitochondrial disulfide relay: Redox-regulated protein import into the intermembrane space
    • Herrmann JM, Riemer J, (2012) Mitochondrial disulfide relay: redox-regulated protein import into the intermembrane space. J Biol Chem 287: 4426-4433
    • (2012) J Biol Chem , vol.287 , pp. 4426-4433
    • Herrmann, J.M.1    Riemer, J.2
  • 20
    • 84868596965 scopus 로고    scopus 로고
    • Intramitochondrial transport of phosphatidic acid in yeast by a lipid transfer protein
    • Connerth M, Tatsuta T, Haag M, Klecker T, Westermann B, Langer T, (2012) Intramitochondrial transport of phosphatidic acid in yeast by a lipid transfer protein. Science 338: 815-818
    • (2012) Science , vol.338 , pp. 815-818
    • Connerth, M.1    Tatsuta, T.2    Haag, M.3    Klecker, T.4    Westermann, B.5    Langer, T.6
  • 22
    • 84881326056 scopus 로고    scopus 로고
    • TRIAP1/PRELI complexes prevent apoptosis by mediating intramitochondrial transport of phosphatidic acid
    • Potting C, Tatsuta T, Konig T, Haag M, Wai T, Aaltonen MJ, Langer T, (2013) TRIAP1/PRELI complexes prevent apoptosis by mediating intramitochondrial transport of phosphatidic acid. Cell Metab 18: 287-295
    • (2013) Cell Metab , vol.18 , pp. 287-295
    • Potting, C.1    Tatsuta, T.2    Konig, T.3    Haag, M.4    Wai, T.5    Aaltonen, M.J.6    Langer, T.7
  • 23
    • 0026544936 scopus 로고
    • Mitochondrial DNA maintenance in yeast requires a protein containing a region related to the GTP-binding domain of dynamin
    • Jones BA, Fangman WL, (1992) Mitochondrial DNA maintenance in yeast requires a protein containing a region related to the GTP-binding domain of dynamin. Genes Dev 6: 380-389
    • (1992) Genes Dev , vol.6 , pp. 380-389
    • Jones, B.A.1    Fangman, W.L.2
  • 24
    • 0033593816 scopus 로고    scopus 로고
    • The yeast dynamin-like protein, mgm1p, functions on the mitochondrial outer membrane to mediate mitochondrial inheritance
    • Shepard KA, Yaffe MP, (1999) The yeast dynamin-like protein, mgm1p, functions on the mitochondrial outer membrane to mediate mitochondrial inheritance. J Cell Biol 144: 711-720
    • (1999) J Cell Biol , vol.144 , pp. 711-720
    • Shepard, K.A.1    Yaffe, M.P.2
  • 25
    • 0038376024 scopus 로고    scopus 로고
    • Mgm1p, a dynamin-related GTPase, is essential for fusion of the mitochondrial outer membrane
    • Sesaki H, Southard SM, Yaffe MP, Jensen RE, (2003) Mgm1p, a dynamin-related GTPase, is essential for fusion of the mitochondrial outer membrane. Mol Biol Cell 14: 2342-2356
    • (2003) Mol Biol Cell , vol.14 , pp. 2342-2356
    • Sesaki, H.1    Southard, S.M.2    Yaffe, M.P.3    Jensen, R.E.4
  • 26
    • 0037415638 scopus 로고    scopus 로고
    • The intramitochondrial dynamin-related GTPase, Mgm1p, is a component of a protein complex that mediates mitochondrial fusion
    • Wong ED, Wagner JA, Scott SV, Okreglak V, Holewinske TJ, Cassidy-Stone A, Nunnari J, (2003) The intramitochondrial dynamin-related GTPase, Mgm1p, is a component of a protein complex that mediates mitochondrial fusion. J Cell Biol 160: 303-311
    • (2003) J Cell Biol , vol.160 , pp. 303-311
    • Wong, E.D.1    Wagner, J.A.2    Scott, S.V.3    Okreglak, V.4    Holewinske, T.J.5    Cassidy-Stone, A.6    Nunnari, J.7
  • 30
    • 80655149471 scopus 로고    scopus 로고
    • Distinct functions of evolutionary conserved MSF1 and late embryogenesis abundant (LEA)-like domains in mitochondria
    • Hall BM, Owens KM, Singh KK, (2011) Distinct functions of evolutionary conserved MSF1 and late embryogenesis abundant (LEA)-like domains in mitochondria. J Biol Chem 286: 39141-39152
    • (2011) J Biol Chem , vol.286 , pp. 39141-39152
    • Hall, B.M.1    Owens, K.M.2    Singh, K.K.3
  • 31
    • 84900417569 scopus 로고    scopus 로고
    • Metabolism and function of mitochondrial cardiolipin
    • Ren M, Phoon CK, Schlame M, (2014) Metabolism and function of mitochondrial cardiolipin. Prog Lipid Res 55: 1-16
    • (2014) Prog Lipid Res , vol.55 , pp. 1-16
    • Ren, M.1    Phoon, C.K.2    Schlame, M.3
  • 32
    • 84895526498 scopus 로고    scopus 로고
    • The topology and regulation of cardiolipin biosynthesis and remodeling in yeast
    • Baile MG, Lu YW, Claypool SM, (2014) The topology and regulation of cardiolipin biosynthesis and remodeling in yeast. Chem Phys Lipids 179: 25-31
    • (2014) Chem Phys Lipids , vol.179 , pp. 25-31
    • Baile, M.G.1    Lu, Y.W.2    Claypool, S.M.3
  • 35
    • 77956365690 scopus 로고    scopus 로고
    • Ups delivery to the intermembrane space of mitochondria: A novel affinity-driven protein import pathway
    • Herrmann JM, (2010) Ups delivery to the intermembrane space of mitochondria: a novel affinity-driven protein import pathway. EMBO J 29: 2859-2860
    • (2010) EMBO J , vol.29 , pp. 2859-2860
    • Herrmann, J.M.1
  • 36
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W, (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol A 276: 307-326
    • (1997) Methods Enzymol A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 38
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley P, Cowtan K, (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr A 60: 2126-2132
    • (2004) Acta Crystallogr A , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 39
    • 0033672549 scopus 로고    scopus 로고
    • Mitochondria-targeted green fluorescent proteins: Convenient tools for the study of organelle biogenesis in Saccharomyces cerevisiae
    • Westermann B, Neupert W, (2000) Mitochondria-targeted green fluorescent proteins: convenient tools for the study of organelle biogenesis in Saccharomyces cerevisiae. Yeast 16: 1421-1427
    • (2000) Yeast , vol.16 , pp. 1421-1427
    • Westermann, B.1    Neupert, W.2
  • 40
    • 0020479718 scopus 로고
    • Import of proteins into mitochondria
    • Daum G, Bohni PC, Schatzg G, (1982) Import of proteins into mitochondria. J Biol Chem 257: 13028-13033
    • (1982) J Biol Chem , vol.257 , pp. 13028-13033
    • Daum, G.1    Bohni, P.C.2    Schatzg, G.3
  • 41
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh EG, Dyer WJ, (1959) A rapid method of total lipid extraction and purification. Can J Biochem Physiol 37: 911-917
    • (1959) Can J Biochem Physiol , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2


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