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Volumn 89, Issue 2-3, 2010, Pages 212-215

The enigmatic role of Mim1 in mitochondrial biogenesis

Author keywords

Mim1; Mitochondria; Structure function relationship; TOM complex assembly

Indexed keywords

MITOCHONDRIAL IMPORT 1; OUTER MEMBRANE PROTEIN; PROTEIN MIM1; UNCLASSIFIED DRUG;

EID: 77149139824     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejcb.2009.11.002     Document Type: Short Survey
Times cited : (14)

References (36)
  • 2
    • 0037070570 scopus 로고    scopus 로고
    • A conserved proline residue is present in the transmembrane-spanning domain of Tom7 and other tail-anchored protein subunits of the TOM translocase
    • Allen R., Egan B., Gabriel K., Beilharz T., Lithgow T. A conserved proline residue is present in the transmembrane-spanning domain of Tom7 and other tail-anchored protein subunits of the TOM translocase. FEBS Lett. 2002, 514:347-350.
    • (2002) FEBS Lett. , vol.514 , pp. 347-350
    • Allen, R.1    Egan, B.2    Gabriel, K.3    Beilharz, T.4    Lithgow, T.5
  • 3
    • 27644467457 scopus 로고    scopus 로고
    • Role of essential genes in mitochondrial morphogenesis in Saccharomyces cerevisiae
    • Altmann K., Westermann B. Role of essential genes in mitochondrial morphogenesis in Saccharomyces cerevisiae. Mol. Biol. Cell 2005, 16:5410-5417.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5410-5417
    • Altmann, K.1    Westermann, B.2
  • 6
    • 0031741738 scopus 로고    scopus 로고
    • Preprotein translocase of the outer mitochondrial membrane: molecular dissection and assembly of the general import pore complex
    • Dekker P.J.T., Ryan M.T., Brix J., Müller H., Hönlinger A., Pfanner N. Preprotein translocase of the outer mitochondrial membrane: molecular dissection and assembly of the general import pore complex. Mol. Cell. Biol. 1998, 18:6515-6524.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6515-6524
    • Dekker, P.J.T.1    Ryan, M.T.2    Brix, J.3    Müller, H.4    Hönlinger, A.5    Pfanner, N.6
  • 8
    • 33746575844 scopus 로고    scopus 로고
    • Evolution of the molecular machines for protein import into mitochondria
    • Dolezal P., Likic V., Tachezy J., Lithgow T. Evolution of the molecular machines for protein import into mitochondria. Science 2006, 313:314-318.
    • (2006) Science , vol.313 , pp. 314-318
    • Dolezal, P.1    Likic, V.2    Tachezy, J.3    Lithgow, T.4
  • 9
    • 0345861754 scopus 로고    scopus 로고
    • The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria
    • Gentle I., Gabriel K., Beech P., Waller R., Lithgow T. The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria. J. Cell Biol. 2004, 164:19-24.
    • (2004) J. Cell Biol. , vol.164 , pp. 19-24
    • Gentle, I.1    Gabriel, K.2    Beech, P.3    Waller, R.4    Lithgow, T.5
  • 10
    • 0032188847 scopus 로고    scopus 로고
    • Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins
    • Hill K., Model K., Ryan M.T., Dietmeier K., Martin F., Wagner R., Pfanner N. Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins. Nature 1998, 395:516-521.
    • (1998) Nature , vol.395 , pp. 516-521
    • Hill, K.1    Model, K.2    Ryan, M.T.3    Dietmeier, K.4    Martin, F.5    Wagner, R.6    Pfanner, N.7
  • 12
    • 4444290664 scopus 로고    scopus 로고
    • Two novel proteins in the mitochondrial outer membrane mediate β-barrel protein assembly
    • Ishikawa D., Yamamoto H., Tamura Y., Moritoh K., Endo T. Two novel proteins in the mitochondrial outer membrane mediate β-barrel protein assembly. J. Cell Biol. 2004, 166:621-627.
    • (2004) J. Cell Biol. , vol.166 , pp. 621-627
    • Ishikawa, D.1    Yamamoto, H.2    Tamura, Y.3    Moritoh, K.4    Endo, T.5
  • 16
    • 67349206741 scopus 로고    scopus 로고
    • The three domains of the mitochondrial outer membrane protein Mim1 have discrete functions in assembly of the TOM complex
    • Lueder F., Lithgow T. The three domains of the mitochondrial outer membrane protein Mim1 have discrete functions in assembly of the TOM complex. FEBS Lett 2009, 583:1475-1480.
    • (2009) FEBS Lett , vol.583 , pp. 1475-1480
    • Lueder, F.1    Lithgow, T.2
  • 19
    • 2542499525 scopus 로고    scopus 로고
    • Sam35 of the mitochondrial protein sorting and assembly machinery is a peripheral outer membrane protein essential for cell viability
    • Milenkovic D., Kozjak V., Wiedemann N., Lohaus C., Meyer H.E., Guiard B., Pfanner N., Meisinger C. Sam35 of the mitochondrial protein sorting and assembly machinery is a peripheral outer membrane protein essential for cell viability. J. Biol. Chem. 2004, 279:22781-22785.
    • (2004) J. Biol. Chem. , vol.279 , pp. 22781-22785
    • Milenkovic, D.1    Kozjak, V.2    Wiedemann, N.3    Lohaus, C.4    Meyer, H.E.5    Guiard, B.6    Pfanner, N.7    Meisinger, C.8
  • 21
    • 0036306343 scopus 로고    scopus 로고
    • Protein translocase of the outer mitochondrial membrane: role of import receptors in the structural organization of the TOM complex
    • Model K., Prinz T., Ruiz T., Radermacher M., Krimmer T., Kuhlbrandt W., Pfanner N., Meisinger C. Protein translocase of the outer mitochondrial membrane: role of import receptors in the structural organization of the TOM complex. J. Mol. Biol. 2002, 316:657-666.
    • (2002) J. Mol. Biol. , vol.316 , pp. 657-666
    • Model, K.1    Prinz, T.2    Ruiz, T.3    Radermacher, M.4    Krimmer, T.5    Kuhlbrandt, W.6    Pfanner, N.7    Meisinger, C.8
  • 22
    • 34249873947 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • Neupert W., Herrmann J.M. Translocation of proteins into mitochondria. Annu. Rev. Biochem. 2007, 76:723-749.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 723-749
    • Neupert, W.1    Herrmann, J.M.2
  • 23
    • 61449229779 scopus 로고    scopus 로고
    • The genetic interactome of prohibitins: coordinated control of cardiolipin and phosphatidylethanolamine by conserved regulators in mitochondria
    • Osman C., Haag M., Potting C., Rodenfels J., Dip P.V., Wieland F.T., Brügger B., Westermann B., Langer T. The genetic interactome of prohibitins: coordinated control of cardiolipin and phosphatidylethanolamine by conserved regulators in mitochondria. J. Cell Biol. 2009, 184:583-596.
    • (2009) J. Cell Biol. , vol.184 , pp. 583-596
    • Osman, C.1    Haag, M.2    Potting, C.3    Rodenfels, J.4    Dip, P.V.5    Wieland, F.T.6    Brügger, B.7    Westermann, B.8    Langer, T.9
  • 25
    • 38649109133 scopus 로고    scopus 로고
    • Mim1 functions in an oligomeric form to facilitate the integration of Tom20 into the mitochondrial outer membrane
    • Popov-Celeketic J., Waizenegger T., Rapaport D. Mim1 functions in an oligomeric form to facilitate the integration of Tom20 into the mitochondrial outer membrane. J. Mol. Biol 2008, 376:671-680.
    • (2008) J. Mol. Biol , vol.376 , pp. 671-680
    • Popov-Celeketic, J.1    Waizenegger, T.2    Rapaport, D.3
  • 26
    • 0036535035 scopus 로고    scopus 로고
    • Biogenesis of the mitochondrial TOM complex
    • Rapaport D. Biogenesis of the mitochondrial TOM complex. Trends Biochem. Sci. 2002, 27:191-197.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 191-197
    • Rapaport, D.1
  • 27
    • 0033606811 scopus 로고    scopus 로고
    • Biogenesis of Tom40, core component of the TOM complex of mitochondria
    • Rapaport D., Neupert W. Biogenesis of Tom40, core component of the TOM complex of mitochondria. J. Cell Biol. 1999, 146:321-331.
    • (1999) J. Cell Biol. , vol.146 , pp. 321-331
    • Rapaport, D.1    Neupert, W.2
  • 28
    • 0034711953 scopus 로고    scopus 로고
    • The GxxxG motif: a framework for transmembrane helix-helix association
    • Russ W.P., Engelman D.M. The GxxxG motif: a framework for transmembrane helix-helix association. J. Mol. Biol. 2000, 296:911-919.
    • (2000) J. Mol. Biol. , vol.296 , pp. 911-919
    • Russ, W.P.1    Engelman, D.M.2
  • 30
    • 4143085058 scopus 로고    scopus 로고
    • Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs
    • Senes A., Engel D.E., DeGrado W.F. Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs. Curr. Opin. Struct. Biol. 2004, 14:465-479.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 465-479
    • Senes, A.1    Engel, D.E.2    DeGrado, W.F.3
  • 32
    • 67449138848 scopus 로고    scopus 로고
    • Ups1p and Ups2p antagonistically regulate cardiolipin metabolism in mitochondria
    • Tamura Y., Endo T., Iijima M., Sesaki H. Ups1p and Ups2p antagonistically regulate cardiolipin metabolism in mitochondria. J. Cell Biol. 2009, 185:1029-1045.
    • (2009) J. Cell Biol. , vol.185 , pp. 1029-1045
    • Tamura, Y.1    Endo, T.2    Iijima, M.3    Sesaki, H.4
  • 34
    • 21444448704 scopus 로고    scopus 로고
    • Mim1, a protein required for the assembly of the TOM complex of mitochondria
    • Waizenegger T., Schmitt S., Zivkovic J., Neupert W., Rapaport D. Mim1, a protein required for the assembly of the TOM complex of mitochondria. EMBO Rep. 2005, 6:57-62.
    • (2005) EMBO Rep. , vol.6 , pp. 57-62
    • Waizenegger, T.1    Schmitt, S.2    Zivkovic, J.3    Neupert, W.4    Rapaport, D.5
  • 35
    • 68949207040 scopus 로고    scopus 로고
    • Biogenesis of β-barrel membrane proteins in bacteria and eukaryotes: evolutionary conservation and divergence
    • Walther D.M., Rapaport D., Tommassen J. Biogenesis of β-barrel membrane proteins in bacteria and eukaryotes: evolutionary conservation and divergence. Cell. Mol. Life Sci. 2009, 66:2789-2804.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 2789-2804
    • Walther, D.M.1    Rapaport, D.2    Tommassen, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.