메뉴 건너뛰기




Volumn 289, Issue 39, 2014, Pages 27352-27362

The mitochondrial ADP/ATP carrier associates with the inner membrane presequence translocase in a stoichiometric manner

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOSYNTHESIS; CELL CULTURE; CELL MEMBRANES; ISOTOPES; METABOLITES; PROTEINS;

EID: 84907584691     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.556498     Document Type: Article
Times cited : (24)

References (52)
  • 1
    • 0037494885 scopus 로고    scopus 로고
    • The cristal membrane of mitochondria is the principal site of oxidative phosphorylation
    • Gilkerson R. W., Selker, J. M., and Capaldi, R. A. (2003) The cristal membrane of mitochondria is the principal site of oxidative phosphorylation. FEBS Lett. 546, 355-358
    • (2003) FEBS Lett , vol.546 , pp. 355-358
    • Gilkerson, R.W.1    Selker, J.M.2    Capaldi, R.A.3
  • 2
    • 33750305666 scopus 로고    scopus 로고
    • Dynamic subcompartmentalization of the mitochondrial inner membrane
    • Vogel, F., Bornhövd, C., Neupert, W., and Reichert, A. S. (2006) Dynamic subcompartmentalization of the mitochondrial inner membrane. J. Cell Biol. 175, 237-247
    • (2006) J. Cell Biol , vol.175 , pp. 237-247
    • Vogel, F.1    Bornhövd, C.2    Neupert, W.3    Reichert, A.S.4
  • 3
    • 33749352547 scopus 로고    scopus 로고
    • Differential protein distributions define two sub-compartments of the mitochondrial inner membrane in yeast
    • Wurm, C. A., and Jakobs, S. (2006) Differential protein distributions define two sub-compartments of the mitochondrial inner membrane in yeast. FEBS Lett. 580, 5628-5634
    • (2006) FEBS Lett , vol.580 , pp. 5628-5634
    • Wurm, C.A.1    Jakobs, S.2
  • 4
    • 57049106773 scopus 로고    scopus 로고
    • Supercomplex organization of the oxidative phosphorylation enzymes in yeast mitochondria
    • Stuart, R. A. (2008) Supercomplex organization of the oxidative phosphorylation enzymes in yeast mitochondria. J. Bioenerg. Biomembr. 40, 411-417
    • (2008) J. Bioenerg. Biomembr , vol.40 , pp. 411-417
    • Stuart, R.A.1
  • 5
    • 67349200007 scopus 로고    scopus 로고
    • Supramolecular organization of ATP synthase and respiratory chain in mitochondrial membranes
    • Wittig, I., and Schägger, H. (2009) Supramolecular organization of ATP synthase and respiratory chain in mitochondrial membranes. Biochim. Biophys. Acta 1787, 672-680
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 672-680
    • Wittig, I.1    Schägger, H.2
  • 7
    • 84871889041 scopus 로고    scopus 로고
    • Biogenesis of mitochondrial carrier proteins: Molecular mechanisms of import into mitochondria
    • Ferramosca, A., and Zara, V. (2013) Biogenesis of mitochondrial carrier proteins: molecular mechanisms of import into mitochondria. Biochim. Biophys. Acta 1833, 494-502
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 494-502
    • Ferramosca, A.1    Zara, V.2
  • 9
    • 52049113898 scopus 로고    scopus 로고
    • The ADP and ATP transport in mitochondria and its carrier
    • Klingenberg, M. (2008) The ADP and ATP transport in mitochondria and its carrier. Biochim. Biophys. Acta 1778, 1978-2021
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1978-2021
    • Klingenberg, M.1
  • 10
    • 77953807486 scopus 로고    scopus 로고
    • Mitochondrial carriers function as monomers
    • Kunji, E. R., and Crichton, P. G. (2010) Mitochondrial carriers function as monomers. Biochim. Biophys. Acta 1797, 817-831
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 817-831
    • Kunji, E.R.1    Crichton, P.G.2
  • 11
    • 62549139614 scopus 로고    scopus 로고
    • Transport of adenine nucleotides in the mitochondria of Saccharomyces cerevisiae: Interactions between the ADP/ATP carriers and the ATP-Mg/Pi carrier
    • Traba, J., Satrústegui, J., and del Arco, A. (2009) Transport of adenine nucleotides in the mitochondria of Saccharomyces cerevisiae: interactions between the ADP/ATP carriers and the ATP-Mg/Pi carrier. Mitochondrion 9, 79-85
    • (2009) Mitochondrion , vol.9 , pp. 79-85
    • Traba, J.1    Satrústegui, J.2    Del Arco, A.3
  • 12
    • 34147113774 scopus 로고    scopus 로고
    • Analysis and prediction of mitochondrial targeting signals
    • Habib, S. J., Neupert, W., and Rapaport, D. (2007) Analysis and prediction of mitochondrial targeting signals. Methods Cell Biol. 80, 761-781
    • (2007) Methods Cell Biol , vol.80 , pp. 761-781
    • Habib, S.J.1    Neupert, W.2    Rapaport, D.3
  • 14
    • 33746575844 scopus 로고    scopus 로고
    • Evolution of the molecular machines for protein import into mitochondria
    • Dolezal, P., Likic, V., Tachezy, J., and Lithgow, T. (2006) Evolution of the molecular machines for protein import into mitochondria. Science 313, 314-318
    • (2006) Science , vol.313 , pp. 314-318
    • Dolezal, P.1    Likic, V.2    Tachezy, J.3    Lithgow, T.4
  • 15
    • 68749112707 scopus 로고    scopus 로고
    • Importing mitochondrial proteins: Machineries and mechanisms
    • Chacinska, A., Koehler, C. M., Milenkovic, D., Lithgow, T., and Pfanner, N. (2009) Importing mitochondrial proteins: machineries and mechanisms. Cell 138, 628-644
    • (2009) Cell , vol.138 , pp. 628-644
    • Chacinska, A.1    Koehler, C.M.2    Milenkovic, D.3    Lithgow, T.4    Pfanner, N.5
  • 16
    • 70349451660 scopus 로고    scopus 로고
    • Multiple pathways for mitochondrial protein traffic
    • Endo, T., and Yamano, K. (2009) Multiple pathways for mitochondrial protein traffic. Biol. Chem. 390, 723-730
    • (2009) Biol. Chem , vol.390 , pp. 723-730
    • Endo, T.1    Yamano, K.2
  • 17
    • 77953807458 scopus 로고    scopus 로고
    • The many faces of the mitochondrial TIM23 complex
    • Mokranjac, D., and Neupert, W. (2010) The many faces of the mitochondrial TIM23 complex. Biochim. Biophys. Acta 1797, 1045-1054
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 1045-1054
    • Mokranjac, D.1    Neupert, W.2
  • 18
    • 84871792997 scopus 로고    scopus 로고
    • Mitochondrial protein import: Common principles and physiological networks
    • Dudek, J., Rehling, P., and van der Laan, M. (2013) Mitochondrial protein import: common principles and physiological networks. Biochim. Biophys. Acta 1833, 274-285
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 274-285
    • Dudek, J.1    Rehling, P.2    Van Der Laan, M.3
  • 20
    • 21244458136 scopus 로고    scopus 로고
    • Role of Tim21 in mitochondrial translocation contact sites
    • Mokranjac, D., Popov-Celeketic, D., Hell, K., and Neupert, W. (2005) Role of Tim21 in mitochondrial translocation contact sites. J. Biol. Chem. 280, 23437-23440
    • (2005) J. Biol. Chem , vol.280 , pp. 23437-23440
    • Mokranjac, D.1    Popov-Celeketic, D.2    Hell, K.3    Neupert, W.4
  • 21
    • 33750949389 scopus 로고    scopus 로고
    • A role for Tim21 in membrane-potential-dependent preprotein sorting in mitochondria
    • van der Laan, M., Wiedemann, N., Mick, D. U., Guiard, B., Rehling, P., and Pfanner, N. (2006) A role for Tim21 in membrane-potential-dependent preprotein sorting in mitochondria. Curr. Biol. 16, 2271-2276
    • (2006) Curr. Biol , vol.16 , pp. 2271-2276
    • Van Der Laan, M.1    Wiedemann, N.2    Mick, D.U.3    Guiard, B.4    Rehling, P.5    Pfanner, N.6
  • 22
    • 37249039150 scopus 로고    scopus 로고
    • Sorting switch of mitochondrial presequence translocase involves coupling of motor module to respiratory chain
    • Wiedemann, N., van der Laan, M., Hutu, D. P., Rehling, P., and Pfanner, N. (2007) Sorting switch of mitochondrial presequence translocase involves coupling of motor module to respiratory chain. J. Cell Biol. 179, 1115-1122
    • (2007) J. Cell Biol , vol.179 , pp. 1115-1122
    • Wiedemann, N.1    Van Der Laan, M.2    Hutu, D.P.3    Rehling, P.4    Pfanner, N.5
  • 23
    • 43749103377 scopus 로고    scopus 로고
    • 1-cytochrome oxidase supercomplex and its association with the TIM23 machinery
    • Saddar, S., Dienhart, M. K., and Stuart, R. A. (2008) The F1Fo-ATP synthase complex influences the assembly state of the cytochrome bc1-cytochrome oxidase supercomplex and its association with the TIM23 machinery. J. Biol. Chem. 283, 6677-6686
    • (2008) J. Biol. Chem , vol.283 , pp. 6677-6686
    • Saddar, S.1    Dienhart, M.K.2    Stuart, R.A.3
  • 24
    • 55549119296 scopus 로고    scopus 로고
    • 1-COX supercomplex and the TIM23 machinery
    • Dienhart, M. K., and Stuart, R. A. (2008) The yeast Aac2 protein exists in physical association with the cytochrome bc1-COX supercomplex and the TIM23 machinery. Mol. Biol. Cell 19, 3934-3943
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3934-3943
    • Dienhart, M.K.1    Stuart, R.A.2
  • 28
  • 29
    • 77955400948 scopus 로고    scopus 로고
    • Cooperation of stop-transfer and conservative sorting mechanisms in mitochondrial protein transport
    • Bohnert, M., Rehling, P., Guiard, B., Herrmann, J. M., Pfanner, N., and van der Laan, M. (2010) Cooperation of stop-transfer and conservative sorting mechanisms in mitochondrial protein transport. Curr. Biol. 20, 1227-1232
    • (2010) Curr. Biol , vol.20 , pp. 1227-1232
    • Bohnert, M.1    Rehling, P.2    Guiard, B.3    Herrmann, J.M.4    Pfanner, N.5    Van Der Laan, M.6
  • 30
    • 84862527999 scopus 로고    scopus 로고
    • The inner-mitochondrial distribution of Oxa1 depends on the growth conditions and on the availability of substrates
    • Stoldt, S., Wenzel, D., Hildenbeutel, M., Wurm, C. A., Herrmann, J. M., and Jakobs, S. (2012) The inner-mitochondrial distribution of Oxa1 depends on the growth conditions and on the availability of substrates. Mol. Biol. Cell 23, 2292-2301
    • (2012) Mol. Biol. Cell , vol.23 , pp. 2292-2301
    • Stoldt, S.1    Wenzel, D.2    Hildenbeutel, M.3    Wurm, C.A.4    Herrmann, J.M.5    Jakobs, S.6
  • 32
    • 63449110220 scopus 로고    scopus 로고
    • Supercomplex organization of the yeast respiratory chain complexes and the ADP/ATP carrier proteins
    • Stuart, R. A. (2009) Supercomplex organization of the yeast respiratory chain complexes and the ADP/ATP carrier proteins. Methods Enzymol. 456, 191-208
    • (2009) Methods Enzymol , vol.456 , pp. 191-208
    • Stuart, R.A.1
  • 33
    • 48749118288 scopus 로고    scopus 로고
    • Mitochondrial protein import motor: Differential role of Tim44 in the recruitment of Pam17 and J-complex to the presequence translocase
    • Hutu, D. P., Guiard, B., Chacinska, A., Becker, D., Pfanner, N., Rehling, P., and van der Laan, M. (2008) Mitochondrial protein import motor: differential role of Tim44 in the recruitment of Pam17 and J-complex to the presequence translocase. Mol. Biol. Cell 19, 2642-2649
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2642-2649
    • Hutu, D.P.1    Guiard, B.2    Chacinska, A.3    Becker, D.4    Pfanner, N.5    Rehling, P.6    Van Der Laan, M.7
  • 41
    • 77952919496 scopus 로고    scopus 로고
    • Identification and functional characterization of a novel mitochondrial carrier for citrate and oxoglutarate in Saccharomyces cerevisiae
    • Castegna, A., Scarcia, P., Agrimi, G., Palmieri, L., Rottensteiner, H., Spera, I., Germinario, L., and Palmieri, F. (2010) Identification and functional characterization of a novel mitochondrial carrier for citrate and oxoglutarate in Saccharomyces cerevisiae. J. Biol. Chem. 285, 17359-17370
    • (2010) J. Biol. Chem , vol.285 , pp. 17359-17370
    • Castegna, A.1    Scarcia, P.2    Agrimi, G.3    Palmieri, L.4    Rottensteiner, H.5    Spera, I.6    Germinario, L.7    Palmieri, F.8
  • 42
  • 43
    • 51649096941 scopus 로고    scopus 로고
    • Cardiolipin defines the interactome of the major ADP/ ATP carrier protein of the mitochondrial inner membrane
    • Claypool, S. M., Oktay, Y., Boontheung, P., Loo, J. A., and Koehler, C. M. (2008) Cardiolipin defines the interactome of the major ADP/ ATP carrier protein of the mitochondrial inner membrane. J. Cell Biol. 182, 937-950
    • (2008) J. Cell Biol , vol.182 , pp. 937-950
    • Claypool, S.M.1    Oktay, Y.2    Boontheung, P.3    Loo, J.A.4    Koehler, C.M.5
  • 45
    • 33846137294 scopus 로고    scopus 로고
    • A cooperative action of the ATP-dependent import motor complex and the inner membrane potential drives mitochondrial preprotein import
    • Krayl, M., Lim, J. H., Martin, F., Guiard, B., and Voos, W. (2007) A cooperative action of the ATP-dependent import motor complex and the inner membrane potential drives mitochondrial preprotein import. Mol. Cell. Biol. 27, 411-425
    • (2007) Mol. Cell. Biol , vol.27 , pp. 411-425
    • Krayl, M.1    Lim, J.H.2    Martin, F.3    Guiard, B.4    Voos, W.5
  • 46
    • 1042266670 scopus 로고    scopus 로고
    • The yeast mitochondrial proteome, a study of fermentative and respiratory growth
    • Ohlmeier, S., Kastaniotis, A. J., Hiltunen, J. K., and Bergmann, U. (2004) The yeast mitochondrial proteome, a study of fermentative and respiratory growth. J. Biol. Chem. 279, 3956-3979
    • (2004) J. Biol. Chem , vol.279 , pp. 3956-3979
    • Ohlmeier, S.1    Kastaniotis, A.J.2    Hiltunen, J.K.3    Bergmann, U.4
  • 47
    • 0027049317 scopus 로고
    • Role of ATP in the intramitochondrial sorting of cytochrome c1 and the adenine nucleotide translocator
    • Wachter, C., Schatz, G., and Glick, B. S. (1992) Role of ATP in the intramitochondrial sorting of cytochrome c1 and the adenine nucleotide translocator. EMBO J. 11, 4787-4794
    • (1992) EMBO J , vol.11 , pp. 4787-4794
    • Wachter, C.1    Schatz, G.2    Glick, B.S.3
  • 48
    • 0028098073 scopus 로고
    • The requirement of matrix ATP for the import of precursor proteins into the mitochondrial matrix and intermembrane space
    • Stuart, R. A., Gruhler, A., van der Klei, I., Guiard, B., Koll, H., and Neupert, W. (1994) The requirement of matrix ATP for the import of precursor proteins into the mitochondrial matrix and intermembrane space. Eur. J. Biochem. 220, 9-18
    • (1994) Eur. J. Biochem , vol.220 , pp. 9-18
    • Stuart, R.A.1    Gruhler, A.2    Van Der Klei, I.3    Guiard, B.4    Koll, H.5    Neupert, W.6
  • 49
    • 0023659499 scopus 로고
    • Mitochondrial proteinimport: Nucleoside triphosphates are involved in conferring importcompetence to precursors
    • Pfanner, N., Tropschug, M., and Neupert, W. (1987) Mitochondrial proteinimport: nucleoside triphosphates are involved in conferring importcompetence to precursors. Cell 49, 815-823
    • (1987) Cell , vol.49 , pp. 815-823
    • Pfanner, N.1    Tropschug, M.2    Neupert, W.3
  • 51
    • 0142105410 scopus 로고    scopus 로고
    • Mitochondrial translocation contact sites: Separation of dynamic and stabilizing elements in formation of a TOM-TIM-preprotein supercomplex
    • Chacinska, A., Rehling, P., Guiard, B., Frazier A. E., Schulze-Specking, A., Pfanner, N., Voos, W., and Meisinger, C. (2003) Mitochondrial translocation contact sites: separation of dynamic and stabilizing elements in formation of a TOM-TIM-preprotein supercomplex. EMBO J. 22, 5370-5381
    • (2003) EMBO J , vol.22 , pp. 5370-5381
    • Chacinska, A.1    Rehling, P.2    Guiard, B.3    Frazier, A.E.4    Schulze-Specking, A.5    Pfanner, N.6    Voos, W.7    Meisinger, C.8
  • 52
    • 0030990662 scopus 로고    scopus 로고
    • 1
    • Giraud, M. F., and Velours, J. (1997) The absence of the mitochondrial ATP synthase δ subunit promotes a slow growth phenotype of rho-yeast cells by a lack of assembly of the catalytic sector F1. Eur. J. Biochem. 245, 813-818
    • (1997) Eur. J. Biochem , vol.245 , pp. 813-818
    • Giraud, M.F.1    Velours, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.