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Volumn 1808, Issue 3, 2011, Pages 971-980

Multiple pathways in the integration of proteins into the mitochondrial outer membrane

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME B5 REDUCTASE; MEMBRANE PROTEIN; MITOCHONDRIAL IMPORT 1; OUTER MEMBRANE PROTEIN; PROTEIN BAK; PROTEIN BAX; PROTEIN BCL XL; TAIL ANCHORED PROTEIN; TRANSLOCASE OF OUTER MITOCHONDRIAL MEMBRANE 20; UNCLASSIFIED DRUG;

EID: 79851513761     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2010.06.021     Document Type: Review
Times cited : (94)

References (119)
  • 1
    • 0031551023 scopus 로고    scopus 로고
    • Phospholipid composition of highly purified mitochondrial outer membranes of rat liver and Neurospora crassa. Is cardiolipin present in the mitochondrial outer membrane?
    • DOI 10.1016/S0005-2736(96)00240-4, PII S0005273696002404
    • A.I.P.M. De Kroon, D. Dolis, A. Mayer, R. Lill, and B. De Kruijff Phospholipid composition of highly purified mitochondrial outer membranes of rat liver and Neurospora crassa. Is cardiolipin present in the mitochondrial outer membrane? Biochim. Biophys. Acta 1325 1997 108 116 (Pubitemid 27138481)
    • (1997) Biochimica et Biophysica Acta - Biomembranes , vol.1325 , Issue.1 , pp. 108-116
    • De Kroon, A.I.P.M.1    Dolis, D.2    Mayer, A.3    Lill, R.4    De Kruijff, B.5
  • 2
    • 0345363228 scopus 로고    scopus 로고
    • Electrospray ionization tandem mass spectrometry (ESI-MS/MS) analysis of the lipid molecular species composition of yeast subcellular membranes reveals acyl chain-based sorting/remodeling of distinct molecular species en route to the plasma membrane
    • DOI 10.1083/jcb.146.4.741
    • R. Schneiter, B. Brugger, R. Sandhoff, G. Zellnig, A. Leber, M. Lampl, K. Athenstaedt, C. Hrastnik, S. Eder, G. Daum, F. Paltauf, F.T. Wieland, and S.D. Kohlwein Electrospray ionization tandem mass spectrometry (ESI-MS/MS) analysis of the lipid molecular species composition of yeast subcellular membranes reveals acyl chain-based sorting/remodeling of distinct molecular species en route to the plasma membrane J. Cell Biol. 146 1999 741 754 (Pubitemid 29408901)
    • (1999) Journal of Cell Biology , vol.146 , Issue.4 , pp. 741-754
    • Schneiter, R.1    Brugger, B.2    Sandhoff, R.3    Zellnig, G.4    Leber, A.5    Lampl, M.6    Athenstaedt, K.7    Hrastnik, C.8    Eder, S.9    Daum, G.10    Paltauf, F.11    Wieland, F.T.12    Kohlwein, S.D.13
  • 3
    • 0026082909 scopus 로고
    • Phospholipid synthesis and lipid composition of subcellular membranes in the unicellular eukaryote Saccharomyces cerevisiae
    • E. Zinser, C.D. Sperka-Gottlieb, E.V. Fasch, S.D. Kohlwein, F. Paltauf, and G. Daum Phospholipid synthesis and lipid composition of subcellular membranes in the unicellular eukaryote Saccharomyces cerevisiae J. Bacteriol. 173 1991 2026 2034
    • (1991) J. Bacteriol. , vol.173 , pp. 2026-2034
    • Zinser, E.1    Sperka-Gottlieb, C.D.2    Fasch, E.V.3    Kohlwein, S.D.4    Paltauf, F.5    Daum, G.6
  • 7
    • 52449116862 scopus 로고    scopus 로고
    • Uncovering the role of VDAC in the regulation of cell life and death
    • V. Shoshan-Barmatz, N. Keinan, and H. Zaid Uncovering the role of VDAC in the regulation of cell life and death J. Bioenerg. Biomembr. 40 2008 183 191
    • (2008) J. Bioenerg. Biomembr. , vol.40 , pp. 183-191
    • Shoshan-Barmatz, V.1    Keinan, N.2    Zaid, H.3
  • 9
    • 57349100367 scopus 로고    scopus 로고
    • Mitofusin 2 tethers endoplasmic reticulum to mitochondria
    • O.M. de Brito, and L. Scorrano Mitofusin 2 tethers endoplasmic reticulum to mitochondria Nature 456 2008 605 610
    • (2008) Nature , vol.456 , pp. 605-610
    • De Brito, O.M.1    Scorrano, L.2
  • 11
    • 0242607644 scopus 로고    scopus 로고
    • Finding the right organelle. Targeting signals in mitochondrial outer-membrane proteins
    • DOI 10.1038/sj.embor.embor937
    • D. Rapaport How to find the right organelle-targeting signals in mitochondrial outer membrane proteins EMBO Rep. 4 2003 948 952 (Pubitemid 37407461)
    • (2003) EMBO Reports , vol.4 , Issue.10 , pp. 948-952
    • Rapaport, D.1
  • 12
    • 0035102443 scopus 로고    scopus 로고
    • Targeting of C-terminal (tail)-anchored proteins: Understanding how cytoplasmic activities are anchored to intracellular membranes
    • DOI 10.1034/j.1600-0854.2001.20108.x
    • B. Wattenberg, and T. Lithgow Targeting of C-terminal (tail)-anchored proteins: understanding how cytoplasmic activities are anchored to intracellular membranes Traffic 2 2001 66 71 (Pubitemid 32219858)
    • (2001) Traffic , vol.2 , Issue.1 , pp. 66-71
    • Wattenberg, B.1    Lithgow, T.2
  • 13
    • 0035911154 scopus 로고    scopus 로고
    • Connection of the mitochondrial outer and inner membranes by Fzo1 is critical for organellar fusion
    • DOI 10.1083/jcb.152.4.683
    • S. Fritz, D. Rapaport, E. Klanner, W. Neupert, and B. Westermann Connection of the mitochondrial outer and inner membranes by Fzo1 is critical for organellar fusion J. Cell Biol. 152 2001 683 692 (Pubitemid 34280154)
    • (2001) Journal of Cell Biology , vol.152 , Issue.4 , pp. 683-692
    • Fritz, S.1    Rapaport, D.2    Klanner, E.3    Neupert, W.4    Westermann, B.5
  • 14
    • 34247340596 scopus 로고    scopus 로고
    • Ugo1p is a multipass transmembrane protein with a single carrier domain required for mitochondrial fusion
    • DOI 10.1111/j.1600-0854.2007.00550.x
    • E.M. Coonrod, M.A. Karren, and J.M. Shaw Ugo1p is a multipass transmembrane protein with a single carrier domain required for mitochondrial fusion Traffic 8 2007 500 511 (Pubitemid 46638562)
    • (2007) Traffic , vol.8 , Issue.5 , pp. 500-511
    • Coonrod, E.M.1    Karren, M.A.2    Shaw, J.M.3
  • 16
    • 47649126755 scopus 로고    scopus 로고
    • Integration of tail-anchored proteins into the mitochondrial outer membrane does not require any known import components
    • DOI 10.1242/jcs.024034
    • C. Kemper, S.J. Habib, G. Engl, P. Heckmeyer, K.S. Dimmer, and D. Rapaport Integration of tail-anchored proteins into the mitochondrial outer membrane does not require any known import components J. Cell Sci. 121 2008 1990 1998 (Pubitemid 352015196)
    • (2008) Journal of Cell Science , vol.121 , Issue.12 , pp. 1990-1998
    • Kemper, C.1    Habib, S.J.2    Engl, G.3    Heckmeyer, P.4    Dimmer, K.S.5    Rapaport, D.6
  • 17
    • 40149096482 scopus 로고    scopus 로고
    • The outer membrane form of the mitochondrial protein Mcr1 follows a TOM-independent membrane insertion pathway
    • B. Meineke, G. Engl, C. Kemper, A. Vasiljev-Neumeyer, H. Paulitschke, and D. Rapaport The outer membrane form of the mitochondrial protein Mcr1 follows a TOM-independent membrane insertion pathway FEBS Lett. 582 2008 855 860
    • (2008) FEBS Lett. , vol.582 , pp. 855-860
    • Meineke, B.1    Engl, G.2    Kemper, C.3    Vasiljev-Neumeyer, A.4    Paulitschke, H.5    Rapaport, D.6
  • 18
    • 33845685298 scopus 로고    scopus 로고
    • Cytosolic factor- and TOM-independent import of C-tail-anchored mitochondrial outer membrane proteins
    • DOI 10.1038/sj.emboj.7601438, PII 7601438
    • K. Setoguchi, H. Otera, and K. Mihara Cytosolic factor- and TOM-independent import of C-tail-anchored mitochondrial outer membrane proteins EMBO J. 25 2006 5635 5647 (Pubitemid 44967748)
    • (2006) EMBO Journal , vol.25 , Issue.24 , pp. 5635-5647
    • Setoguchi, K.1    Otera, H.2    Mihara, K.3
  • 19
  • 20
    • 0035099421 scopus 로고    scopus 로고
    • Protein import channel of the outer mitochondrial membrane: A highly stable Tom40-Tom22 core structure differentially interacts with preproteins, small Tom proteins, and import receptors
    • DOI 10.1128/MCB.21.7.2337-2348.2001
    • C. Meisinger, M.T. Ryan, K. Hill, K. Model, J.H. Lim, A. Sickmann, H. Muller, H.E. Meyer, R. Wagner, and N. Pfanner Protein import channel of the outer mitochondrial membrane: a highly stable Tom40-Tom22 core structure differentially interacts with preproteins, small tom proteins, and import receptors Mol. Cell. Biol. 21 2001 2337 2348 (Pubitemid 32222087)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.7 , pp. 2337-2348
    • Meisinger, C.1    Ryan, M.T.2    Hill, K.3    Model, K.4    Lim, J.H.5    Sickmann, A.6    Muller, H.7    Meyer, H.E.8    Wagner, R.9    Pfanner, N.10
  • 21
    • 0035115121 scopus 로고    scopus 로고
    • Purification and characterization of the preprotein translocase of the outer mitochondrial membrane from Arabidopsis. Identification of multiple forms of TOM20
    • DOI 10.1104/pp.125.2.943
    • W. Werhahn, A. Niemeyer, L. Jansch, V. Kruft, U.K. Schmitz, and H. Braun Purification and characterization of the preprotein translocase of the outer mitochondrial membrane from Arabidopsis. Identification of multiple forms of TOM20 Plant Physiol. 125 2001 943 954 (Pubitemid 32169901)
    • (2001) Plant Physiology , vol.125 , Issue.2 , pp. 943-954
    • Werhahn, W.1    Niemeyer, A.2    Jansch, L.3    Kruft, V.4    Schmitz, U.K.5    Braun, H.-P.6
  • 25
    • 0036306343 scopus 로고    scopus 로고
    • Protein translocase of the outer mitochondrial membrane: Role of import receptors in the structural organization of the TOM complex
    • DOI 10.1006/jmbi.2001.5365
    • K. Model, T. Prinz, T. Ruiz, M. Radermacher, T. Krimmer, W. Kuhlbrandt, N. Pfanner, and C. Meisinger Protein translocase of the outer mitochondrial membrane: role of import receptors in the structural organization of the TOM complex J. Mol. Biol. 316 2002 657 666 (Pubitemid 34729247)
    • (2002) Journal of Molecular Biology , vol.316 , Issue.3 , 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
  • 26
    • 0035844870 scopus 로고    scopus 로고
    • Tom40, the pore-forming component of the protein-conducting TOM channel in the outer membrane of mitochondria
    • DOI 10.1083/jcb.153.6.1151
    • U. Ahting, M. Thieffry, H. Engelhardt, R. Hegerl, W. Neupert, and S. Nussberger Tom40, the pore-forming component of the protein-conducting TOM channel in the outer membrane of mitochondria J. Cell Biol. 153 2001 1151 1160 (Pubitemid 34289255)
    • (2001) Journal of Cell Biology , vol.153 , Issue.6 , pp. 1151-1160
    • Ahting, U.1    Thieffry, M.2    Engelhardt, H.3    Hegerl, R.4    Neupert, W.5    Nussberger, S.6
  • 27
    • 0032188847 scopus 로고    scopus 로고
    • Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins
    • DOI 10.1038/26780
    • K. Hill, K. Model, M.T. Ryan, K. Dietmeier, F. Martin, R. Wagner, and N. Pfanner Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins Nature 395 1998 516 521 (Pubitemid 28462448)
    • (1998) Nature , vol.395 , Issue.6701 , pp. 516-521
    • Hill, K.1    Model, K.2    Ryan, M.T.3    Dietmeier, K.4    Martint, F.5    Wagner, R.6    Pfanner, N.7
  • 30
    • 0345189360 scopus 로고    scopus 로고
    • Tom40 protein import channel binds to non-native proteins and prevents their aggregation
    • DOI 10.1038/nsb1008
    • M. Esaki, T. Kanamori, S. Nishikawa, I. Shin, P.G. Schultz, and T. Endo Tom40 protein import channel binds to non-native proteins and prevents their aggregation Nat. Struct. Biol. 10 2003 988 994 (Pubitemid 37500490)
    • (2003) Nature Structural Biology , vol.10 , Issue.12 , pp. 988-994
    • Esaki, M.1    Kanamori, T.2    Nishikawa, S.-I.3    Shin, I.4    Schultz, P.G.5    Endo, T.6
  • 33
    • 0029156778 scopus 로고
    • MOM22 is a receptor for mitochondrial targeting sequences and cooperates with MOM19
    • A. Mayer, F.E. Nargang, W. Neupert, and R. Lill MOM22 is a receptor for mitochondrial targeting sequences and cooperates with MOM19 EMBO J. 14 1995 4204 4211
    • (1995) EMBO J. , vol.14 , pp. 4204-4211
    • Mayer, A.1    Nargang, F.E.2    Neupert, W.3    Lill, R.4
  • 34
    • 0033620612 scopus 로고    scopus 로고
    • Direct membrane insertion of voltage-dependent anion-selective channel protein catalyzed by mitochondrial Tom20
    • DOI 10.1083/jcb.145.5.973
    • E. Schleiff, J.R. Silvius, and G.C. Shore Direct membrane insertion of voltage-dependent anion-selective channel protein catalyzed by mitochondrial Tom20 J. Cell Biol. 145 1999 973 978 (Pubitemid 29270056)
    • (1999) Journal of Cell Biology , vol.145 , Issue.5 , pp. 973-978
    • Schleiff, E.1    Silvius, J.R.2    Shore, G.C.3
  • 35
    • 42949139525 scopus 로고    scopus 로고
    • Tom20 and Tom22 share the common signal recognition pathway in mitochondrial protein import
    • K. Yamano, Y. Yatsukawa, M. Esaki, A.E. Hobbs, R.E. Jensen, and T. Endo Tom20 and Tom22 share the common signal recognition pathway in mitochondrial protein import J. Biol. Chem. 283 2008 3799 3807
    • (2008) J. Biol. Chem. , vol.283 , pp. 3799-3807
    • Yamano, K.1    Yatsukawa, Y.2    Esaki, M.3    Hobbs, A.E.4    Jensen, R.E.5    Endo, T.6
  • 36
    • 0040610676 scopus 로고    scopus 로고
    • Distribution of binding sequences for the mitochondrial import receptors Tom20, Tom22, and Tom70 in a presequence-carrying preprotein and a non-cleavable preprotein
    • J. Brix, S. Rudiger, B. Bukau, J. Schneider-Mergener, and N. Pfanner Distribution of binding sequences for the mitochondrial import receptors Tom20, Tom22, and Tom70 in a presequence-carrying preprotein and a non-cleavable preprotein J. Biol. Chem. 274 1999 16522 16530
    • (1999) J. Biol. Chem. , vol.274 , pp. 16522-16530
    • Brix, J.1    Rudiger, S.2    Bukau, B.3    Schneider-Mergener, J.4    Pfanner, N.5
  • 37
    • 0028365278 scopus 로고
    • Specific recognition of mitochondrial preproteins by the cytosolic domain of the import receptor MOM72
    • J. Schlossmann, K. Dietmeier, N. Pfanner, and W. Neupert Specific recognition of mitochondrial preproteins by the cytosolic domain of the import receptor MOM72 J. Biol. Chem. 269 1994 11893 11901 (Pubitemid 24196678)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.16 , pp. 11893-11901
    • Schlossmann, J.1    Dietmeier, K.2    Pfanner, N.3    Neupert, W.4
  • 42
    • 0028862969 scopus 로고
    • The mitochondrial receptor complex: The small subunit Mom8b/Isp6 supports association of receptors with the general insertion pore and transfer of preproteins
    • A. Alconada, M. Kübrich, M. Moczko, A. Hönlinger, and N. Pfanner The mitochondrial receptor complex: the small subunit Mom8b/Isp6 supports association of receptors with the general insertion pore and transfer of preproteins Mol. Cell. Biol. 15 1995 6196 6205
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6196-6205
    • Alconada, A.1    Kübrich, M.2    Moczko, M.3    Hönlinger, A.4    Pfanner, N.5
  • 45
    • 24344508557 scopus 로고    scopus 로고
    • Functions of the small proteins in the TOM complex of Neurospora crasssa
    • DOI 10.1091/mbc.E05-03-0187
    • E.L. Sherman, N.E. Go, and F.E. Nargang Functions of the small proteins in the TOM complex of Neurospora crasssa Mol. Biol. Cell 16 2005 4172 4182 (Pubitemid 41262887)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.9 , pp. 4172-4182
    • Sherman, E.L.1    Go, N.E.2    Nargang, F.E.3
  • 46
    • 0041428149 scopus 로고    scopus 로고
    • The versatile beta-barrel membrane protein
    • W.C. Wimley The versatile beta-barrel membrane protein Curr. Opin. Struct. Biol. 13 2003 404 411
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 404-411
    • Wimley, W.C.1
  • 47
    • 68949207040 scopus 로고    scopus 로고
    • Biogenesis of β-barrel membrane proteins in bacteria and eukaryotes: Evolutionary conservation and divergence
    • D.M. Walther, D. Rapaport, and J. Tommassen Biogenesis of β-barrel membrane proteins in bacteria and eukaryotes: evolutionary conservation and divergence Cell. Mol. Life Sci. 66 2009 2789 2804
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 2789-2804
    • Walther, D.M.1    Rapaport, D.2    Tommassen, J.3
  • 48
    • 0033942874 scopus 로고    scopus 로고
    • Structure and function of bacterial outer membrane proteins: Barrels in a nutshell
    • DOI 10.1046/j.1365-2958.2000.01983.x
    • R. Koebnik, K.P. Locher, and P. Van Gelder Structure and function of bacterial outer membrane proteins: barrels in a nutshell Mol. Microbiol. 37 2000 239 253 (Pubitemid 30481009)
    • (2000) Molecular Microbiology , vol.37 , Issue.2 , pp. 239-253
    • Koebnik, R.1    Locher, K.P.2    Van Gelder, P.3
  • 49
    • 25144452723 scopus 로고    scopus 로고
    • Biogenesis of β-barrel membrane proteins of mitochondria
    • DOI 10.1016/j.tibs.2005.08.009, PII S0968000405002410
    • S.A. Paschen, W. Neupert, and D. Rapaport Biogenesis of beta-barrel membrane proteins of mitochondria Trends Biochem. Sci. 30 2005 575 582 (Pubitemid 41356496)
    • (2005) Trends in Biochemical Sciences , vol.30 , Issue.10 , pp. 575-582
    • Paschen, S.A.1    Neupert, W.2    Rapaport, D.3
  • 51
    • 0028024592 scopus 로고
    • Regulation of mitochondrial morphology and inheritance by Mdm10p, a protein of the mitochondrial outer membrane
    • L.F. Sogo, and M.P. Yaffe Regulation of mitochondrial morphology and inheritance by Mdm10p, a protein of the mitochondrial outer membrane J. Cell Biol. 130 1994 1361 1373 (Pubitemid 24284603)
    • (1994) Journal of Cell Biology , vol.126 , Issue.6 , pp. 1361-1373
    • Sogo, L.F.1    Yaffe, M.P.2
  • 53
    • 0033606811 scopus 로고    scopus 로고
    • Biogenesis of Tom40, core component of the TOM complex of mitochondria
    • DOI 10.1083/jcb.146.2.321
    • D. Rapaport, and W. Neupert Biogenesis of Tom40, core component of the TOM complex of mitochondria J. Cell Biol. 146 1999 321 331 (Pubitemid 29369770)
    • (1999) Journal of Cell Biology , vol.146 , Issue.2 , pp. 321-331
    • Rapaport, D.1    Neupert, W.2
  • 54
    • 0030586353 scopus 로고    scopus 로고
    • Role of the N- and C-termini of porin in import into the outer membrane of Neurospora mitochondria
    • DOI 10.1016/0014-5793(96)00629-1
    • D.A. Court, R. Kleene, W. Neupert, and R. Lill Role of the N- and C-termini of porin in import into the outer membrane of Neurospora mitochondria FEBS Lett. 390 1996 73 77 (Pubitemid 26233270)
    • (1996) FEBS Letters , vol.390 , Issue.1 , pp. 73-77
    • Court, D.A.1    Kleene, R.2    Neupert, W.3    Lill, R.4
  • 56
    • 62449307987 scopus 로고    scopus 로고
    • Signals in bacterial b-barrel proteins are functional in eukaryotic cells for targeting to and assembly in mitochondria
    • D.M. Walther, D. Papic, M.P. Bos, J. Tommassen, and D. Rapaport Signals in bacterial b-barrel proteins are functional in eukaryotic cells for targeting to and assembly in mitochondria Proc. Natl. Acad. Sci. USA 106 2009 2531 2536
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 2531-2536
    • Walther, D.M.1    Papic, D.2    Bos, M.P.3    Tommassen, J.4    Rapaport, D.5
  • 59
    • 1842478040 scopus 로고    scopus 로고
    • The Tim8-Tim13 Complex of Neurospora crassa Functions in the Assembly of Proteins into Both Mitochondrial Membranes
    • DOI 10.1074/jbc.M313037200
    • S.C. Hoppins, and F.E. Nargang The Tim8-Tim13 complex of Neurospora crassa functions in the assembly of proteins into both mitochondrial membranes J. Biol. Chem. 279 2004 12396 12405 (Pubitemid 38445807)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.13 , pp. 12396-12405
    • Hoppins, S.C.1    Nargang, F.E.2
  • 60
    • 2442421175 scopus 로고    scopus 로고
    • Biogenesis of the protein import channel Tom40 of the mitochondrial outer membrane: Intermembrane space components are involved in an early stage of the assembly pathway
    • DOI 10.1074/jbc.M400050200
    • N. Wiedemann, K.N. Truscott, S. Pfannschmidt, B. Guiard, C. Meisinger, and N. Pfanner Biogenesis of the protein import channel Tom40 of the mitochondrial outer membrane: intermembrane space components are involved in an early stage of the assembly pathway J. Biol. Chem. 279 2004 18188 18194 (Pubitemid 38623231)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.18 , pp. 18188-18194
    • Wiedemann, N.1    Truscott, K.N.2    Pfannschmidt, S.3    Guiard, B.4    Meisinger, C.5    Pfanner, N.6
  • 61
    • 0028149597 scopus 로고
    • Rupture of the mitochondrial outer membrane impairs porin assembly
    • M. Smith, S. Hicks, K. Baker, and R. McCauley Rupture of the mitochondrial outer membrane impairs porin assembly J. Biol. Chem. 269 1994 28460 28464 (Pubitemid 24354592)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.45 , pp. 28460-28464
    • Smith, M.1    Hicks, S.2    Baker, K.3    McCauley, R.4
  • 62
    • 0345861754 scopus 로고    scopus 로고
    • The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria
    • DOI 10.1083/jcb.200310092
    • I. Gentle, K. Gabriel, P. Beech, R. Waller, and T. Lithgow The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria J. Cell Biol. 164 2004 19 24 (Pubitemid 38082453)
    • (2004) Journal of Cell Biology , vol.164 , Issue.1 , pp. 19-24
    • Gentle, I.1    Gabriel, K.2    Beech, P.3    Waller, R.4    Lithgow, T.5
  • 64
    • 2542499525 scopus 로고    scopus 로고
    • Sam35 of the mitochondrial protein sorting and assembly machinery is a peripheral outer membrane protein essential for cell viability
    • DOI 10.1074/jbc.C400120200
    • D. Milenkovic, V. Kozjak, N. Wiedemann, C. Lohaus, H.E. Meyer, B. Guiard, N. Pfanner, and C. Meisinger Sam35 of the mitochondrial protein sorting and assembly machinery is a peripheral outer membrane protein essential for cell viability J. Biol. Chem. 279 2004 22781 22785 (Pubitemid 38679479)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.21 , 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
  • 65
    • 4444376183 scopus 로고    scopus 로고
    • Tob38, a novel essential component in the biogenesis of β-barrel proteins of mitochondria
    • DOI 10.1038/sj.embor.7400183
    • T. Waizenegger, S.J. Habib, M. Lech, D. Mokranjac, S.A. Paschen, K. Hell, W. Neupert, and D. Rapaport Tob38, a novel essential component in the biogenesis of beta-barrel proteins of mitochondria EMBO Rep. 5 2004 704 709 (Pubitemid 39173006)
    • (2004) EMBO Reports , vol.5 , Issue.7 , pp. 704-709
    • Waizenegger, T.1    Habib, S.J.2    Lech, M.3    Mokranjac, D.4    Paschen, S.A.5    Hell, K.6    Neupert, W.7    Rapaport, D.8
  • 68
    • 4444290664 scopus 로고    scopus 로고
    • Two novel proteins in the mitochondrial outer membrane mediate β-barrel protein assembly
    • DOI 10.1083/jcb.200405138
    • D. Ishikawa, H. Yamamoto, Y. Tamura, K. Moritoh, and T. Endo Two novel proteins in the mitochondrial outer membrane mediate beta-barrel protein assembly J. Cell Biol. 166 2004 621 627 (Pubitemid 39180999)
    • (2004) Journal of Cell Biology , vol.166 , Issue.5 , pp. 621-627
    • Ishikawa, D.1    Yamamoto, H.2    Tamura, Y.3    Moritoh, K.4    Endo, T.5
  • 69
    • 0036305169 scopus 로고    scopus 로고
    • A Toc75-like protein import channel is abundant in chloroplasts
    • DOI 10.1093/embo-reports/kvf110
    • K. Eckart, L. Eichacker, K. Sohrt, E. Schleiff, L. Heins, and J. Soll A Toc75-like protein import channel is abundant in chloroplasts EMBO Rep. 3 2002 557 562 (Pubitemid 34752456)
    • (2002) EMBO Reports , vol.3 , Issue.6 , pp. 557-562
    • Eckart, K.1    Eichacker, L.2    Sohrt, K.3    Schleiff, E.4    Heins, L.5    Soll, J.6
  • 70
    • 1842471109 scopus 로고    scopus 로고
    • Omp85, an evolutionarily conserved bacterial protein involved in outer-membrane-protein assembly
    • DOI 10.1016/j.resmic.2003.11.007, PII S0923250803002778
    • R. Voulhoux, and J. Tommassen Omp85, an evolutionarily conserved bacterial protein involved in outer-membrane-protein assembly Res. Microbiol. 155 2004 129 135 (Pubitemid 38430024)
    • (2004) Research in Microbiology , vol.155 , Issue.3 , pp. 129-135
    • Voulhoux, R.1    Tommassen, J.2
  • 71
    • 0642377467 scopus 로고    scopus 로고
    • POTRA: A conserved domain in the FtsQ family and a class of β-barrel outer membrane proteins
    • DOI 10.1016/j.tibs.2003.08.003, PII S0968000403002123
    • L. Sanchez-Pulido, D. Devos, S. Genevrois, M. Vicente, and A. Valencia POTRA: a conserved domain in the FtsQ family and a class of beta-barrel outer membrane proteins Trends Biochem. Sci. 28 2003 523 526 (Pubitemid 38366276)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.10 , pp. 523-526
    • Sanchez-Pulido, L.1    Devos, D.2    Genevrois, S.3    Vicente, M.4    Valencia, A.5
  • 72
    • 34548139422 scopus 로고    scopus 로고
    • Structure and function of an essential component of the outer membrane protein assembly machine
    • DOI 10.1126/science.1143993
    • S. Kim, J.C. Malinverni, P. Sliz, T.J. Silhavy, S.C. Harrison, and D. Kahne Structure and function of an essential component of the outer membrane protein assembly machine Science 317 2007 961 964 (Pubitemid 47301326)
    • (2007) Science , vol.317 , Issue.5840 , pp. 961-964
    • Kim, S.1    Malinverni, J.C.2    Sliz, P.3    Silhavy, T.J.4    Harrison, S.C.5    Kahne, D.6
  • 73
    • 33751056360 scopus 로고    scopus 로고
    • Assembly factor Omp85 recognizes its outer membrane protein substrates by a species-specific C-terminal motif
    • V. Robert, E.B. Volokhina, F. Senf, M.P. Bos, P. Van Gelder, and J. Tommassen Assembly factor Omp85 recognizes its outer membrane protein substrates by a species-specific C-terminal motif PLoS Biol. 4 2006 e377
    • (2006) PLoS Biol. , vol.4 , pp. 377
    • Robert, V.1    Volokhina, E.B.2    Senf, F.3    Bos, M.P.4    Van Gelder, P.5    Tommassen, J.6
  • 74
    • 33846002342 scopus 로고    scopus 로고
    • The N-terminal domain of Tob55 has a receptor-like function in the biogenesis of mitochondrial β-barrel proteins
    • DOI 10.1083/jcb.200602050
    • S.J. Habib, T. Waizenegger, A. Niewienda, S.A. Paschen, W. Neupert, and D. Rapaport The N-terminal domain of Tob55 has a receptor-like function in the biogenesis of mitochondrial beta-barrel proteins J. Cell Biol. 176 2007 77 88 (Pubitemid 46041682)
    • (2007) Journal of Cell Biology , vol.176 , Issue.1 , pp. 77-88
    • Habib, S.J.1    Waizenegger, T.2    Niewienda, A.3    Paschen, S.A.4    Neupert, W.5    Rapaport, D.6
  • 75
    • 38749085210 scopus 로고    scopus 로고
    • The peripheral membrane subunits of the SAM complex function codependently in mitochondrial outer membrane biogenesis
    • DOI 10.1091/mbc.E07-08-0796
    • N.C. Chan, and T. Lithgow The peripheral membrane subunits of the SAM complex function codependently in mitochondrial outer membrane biogenesis Mol. Biol. Cell 19 2008 126 136 (Pubitemid 351186139)
    • (2008) Molecular Biology of the Cell , vol.19 , Issue.1 , pp. 126-136
    • Chan, N.C.1    Lithgow, T.2
  • 76
    • 34547688974 scopus 로고    scopus 로고
    • Conserved roles of Sam50 and metaxins in VDAC biogenesis
    • DOI 10.1038/sj.embor.7400982, PII 7400982
    • V. Kozjak-Pavlovic, K. Ross, N. Benlasfer, S. Kimmig, A. Karlas, and T. Rudel Conserved roles of Sam50 and metaxins in VDAC biogenesis EMBO Rep. 8 2007 576 582 (Pubitemid 47214712)
    • (2007) EMBO Reports , vol.8 , Issue.6 , pp. 576-582
    • Kozjak-Pavlovic, V.1    Ross, K.2    Benlasfer, N.3    Kimmig, S.4    Karlas, A.5    Rudel, T.6
  • 77
    • 71949129385 scopus 로고    scopus 로고
    • Genetic and functional interactions between the mitochondrial outer membrane proteins Tom6 and Sam37
    • J. Dukanovic, K.S. Dimmer, N. Bonnefoy, K. Krumpe, and D. Rapaport Genetic and functional interactions between the mitochondrial outer membrane proteins Tom6 and Sam37 Mol. Cell. Biol. 29 2009 5975 5988
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 5975-5988
    • Dukanovic, J.1    Dimmer, K.S.2    Bonnefoy, N.3    Krumpe, K.4    Rapaport, D.5
  • 78
    • 0344392841 scopus 로고    scopus 로고
    • A Protein Complex Containing Mdm10p, Mdm12p, and Mmm1p Links Mitochondrial Membranes and DNA to the Cytoskeleton-based Segregation Machinery
    • DOI 10.1091/mbc.E03-04-0225
    • I.R. Boldogh, D.W. Nowakowski, H.C. Yang, H. Chung, S. Karmon, P. Royes, and L.A. Pon A protein complex containing Mdm10p, Mdm12p, and Mmm1p links mitochondrial membranes and DNA to the cytoskeleton-based segregation machinery Mol. Biol. Cell 14 2003 4618 4627 (Pubitemid 37444660)
    • (2003) Molecular Biology of the Cell , vol.14 , Issue.11 , pp. 4618-4627
    • Boldogh, I.R.1    Nowakowski, D.W.2    Yang, H.-C.3    Chung, H.4    Karmon, S.5    Royes, P.6    Pon, L.A.7
  • 79
    • 77649274082 scopus 로고    scopus 로고
    • Mdm10 as a dynamic constituent of the TOB/SAM complex directs coordinated assembly of Tom40
    • K. Yamano, S. Tanaka-Yamano, and T. Endo Mdm10 as a dynamic constituent of the TOB/SAM complex directs coordinated assembly of Tom40 EMBO Rep. 11 2010 187 193
    • (2010) EMBO Rep. , vol.11 , pp. 187-193
    • Yamano, K.1    Tanaka-Yamano, S.2    Endo, T.3
  • 83
    • 0024818131 scopus 로고
    • The major 45-kDa protein of the yeast mitochondrial outer membrane is not essential for cell growth or mitochondrial function
    • M.P. Yaffe, R.E. Jensen, and E.C. Guido The major 45-kDa protein of the yeast mitochondrial outer membrane is not essential for cell growth or mitochondrial function J. Biol. Chem. 264 1989 21091 21096 (Pubitemid 20017922)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.35 , pp. 21091-21096
    • Yaffe, M.P.1    Jensen, R.E.2    Guido, E.C.3
  • 84
    • 0027940215 scopus 로고
    • 5 reductase to two different submitochondrial compartments
    • DOI 10.1016/0092-8674(94)90072-8
    • K. Hahne, V. Haucke, L. Ramage, and G. Schatz Incomplete arrest in the outer membrane sorts NADH-cytochrome b5 reductase to two different submitochondrial compartments Cell 79 1994 829 839 (Pubitemid 24371973)
    • (1994) Cell , vol.79 , Issue.5 , pp. 829-839
    • Hahne, K.1    Haucke, V.2    Ramage, L.3    Schatz, G.4
  • 85
    • 0142242210 scopus 로고    scopus 로고
    • Signal-anchor domains of proteins of the outer membrane of mitochondria: Structural and functional characteristics
    • DOI 10.1074/jbc.M305736200
    • T. Waizenegger, T. Stan, W. Neupert, and D. Rapaport Signal-anchor domains of proteins of the outer membrane of mitochondria: structural and functional characteristics J. Biol. Chem. 278 2003 42064 42071 (Pubitemid 37310472)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.43 , pp. 42064-42071
    • Waizenegger, T.1    Stan, T.2    Neupert, W.3    Rapaport, D.4
  • 86
    • 0034675885 scopus 로고    scopus 로고
    • Characterization of the signal that directs Tom20 to the mitochondrial outer membrane
    • S. Kanaji, J. Iwahashi, Y. Kida, M. Sakaguchi, and K. Mihara Characterization of the signal that directs Tom20 to the mitochondrial outer membrane J. Cell Biol. 151 2000 277 288
    • (2000) J. Cell Biol. , vol.151 , pp. 277-288
    • Kanaji, S.1    Iwahashi, J.2    Kida, Y.3    Sakaguchi, M.4    Mihara, K.5
  • 87
    • 0036558288 scopus 로고    scopus 로고
    • Characterization of rat TOM70 as a receptor of the preprotein translocase of the mitochondrial outer membrane
    • H. Suzuki, M. Maeda, and K. Mihara Characterization of rat TOM70 as a receptor of the preprotein translocase of the mitochondrial outer membrane J. Cell Sci. 115 2002 1895 1905 (Pubitemid 34567251)
    • (2002) Journal of Cell Science , vol.115 , Issue.9 , pp. 1895-1905
    • Suzuki, H.1    Maeda, M.2    Mihara, K.3
  • 88
    • 0028803669 scopus 로고
    • Assembly of the preprotein receptor MOM72/MAS70 into the protein import complex of the outer membrane of mitochondria
    • J. Schlossmann, and W. Neupert Assembly of the preprotein receptor MOM72/MAS70 into the protein import complex of the outer membrane of mitochondria J. Biol. Chem. 270 1995 27116 27121
    • (1995) J. Biol. Chem. , vol.270 , pp. 27116-27121
    • Schlossmann, J.1    Neupert, W.2
  • 90
    • 12844276571 scopus 로고    scopus 로고
    • Signal-anchored proteins follow a unique insertion pathway into the outer membrane of mitochondria
    • DOI 10.1074/jbc.M410905200
    • U. Ahting, T. Waizenegger, W. Neupert, and D. Rapaport Signal-anchored proteins follow a unique insertion pathway into the outer membrane of mitochondria J. Biol. Chem. 280 2005 48 53 (Pubitemid 40164963)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.1 , pp. 48-53
    • Ahting, U.1    Waizenegger, T.2    Neupert, W.3    Rapaport, D.4
  • 92
    • 21444448704 scopus 로고    scopus 로고
    • Mim1, a protein required for the assembly of the TOM complex of mitochondria
    • DOI 10.1038/sj.embor.7400318
    • T. Waizenegger, S. Schmitt, J. Zivkovic, W. Neupert, and D. Rapaport Mim1, a protein required for the assembly of the TOM complex of mitochondria EMBO Rep. 6 2005 57 62 (Pubitemid 41710075)
    • (2005) EMBO Reports , vol.6 , Issue.1 , pp. 57-62
    • Waizenegger, T.1    Schmitt, S.2    Zivkovic, J.3    Neupert, W.4    Rapaport, D.5
  • 95
    • 38649109133 scopus 로고    scopus 로고
    • Mim1 functions in an oligomeric form to facilitate the integration of Tom20 into the mitochondrial outer membrane
    • J. Popov-Celeketic, T. Waizenegger, and D. Rapaport Mim1 functions in an oligomeric form to facilitate the integration of Tom20 into the mitochondrial outer membrane J. Mol. Biol. 376 2008 671 680
    • (2008) J. Mol. Biol. , vol.376 , pp. 671-680
    • Popov-Celeketic, J.1    Waizenegger, T.2    Rapaport, D.3
  • 96
    • 34547937485 scopus 로고    scopus 로고
    • How tails guide tail-anchored proteins to their destinations
    • DOI 10.1016/j.ceb.2007.04.019, PII S0955067407000877
    • N. Borgese, S. Brambillasca, and S. Colombo How tails guide tail-anchored proteins to their destinations Curr. Opin. Cell Biol. 19 2007 368 375 (Pubitemid 47268760)
    • (2007) Current Opinion in Cell Biology , vol.19 , Issue.4 , pp. 368-375
    • Borgese, N.1    Brambillasca, S.2    Colombo, S.3
  • 97
    • 0036000002 scopus 로고    scopus 로고
    • Characterization of signal that directs C-tail-anchored proteins to mammalian mitochondrial outer membrane
    • DOI 10.1091/mbc.01-12-0570
    • C. Horie, H. Suzuki, M. Sakaguchi, and K. Mihara Characterization of signal that directs C-tail-anchored proteins to mammalian mitochondrial outer membrane Mol. Biol. Cell 13 2002 1615 1625 (Pubitemid 34522643)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.5 , pp. 1615-1625
    • Horie, C.1    Suzuki, H.2    Sakaguchi, M.3    Mihara, K.4
  • 98
    • 0031871330 scopus 로고    scopus 로고
    • A splice-isoform of vesicle-associated membrane protein-1 (VAMP-1) contains a mitochondrial targeting signal
    • S. Isenmann, Y. Khew-Goodall, J. Gamble, M. Vadas, and B.W. Wattenberg A splice-isoform of vesicle-associated membrane protein-1 (VAMP-1) contains a mitochondrial targeting signal Mol. Biol. Cell 9 1998 1649 1660 (Pubitemid 28337513)
    • (1998) Molecular Biology of the Cell , vol.9 , Issue.7 , pp. 1649-1660
    • Isenmann, S.1    Khew-Goodall, Y.2    Gamble, J.3    Vadas, M.4    Wattenberg, B.W.5
  • 100
    • 0142039790 scopus 로고    scopus 로고
    • Targeting and Assembly of Mitochondrial Tail-anchored Protein Tom5 to the TOM Complex Depend on a Signal Distinct from That of Tail-anchored Proteins Dispersed in the Membrane
    • DOI 10.1074/jbc.M307047200
    • C. Horie, H. Suzuki, M. Sakaguchi, and K. Mihara Targeting and assembly of mitochondrial tail-anchored protein Tom5 to the TOM complex depend on a signal distinct from that of tail-anchored proteins dispersed in the membrane J. Biol. Chem. 278 2003 41462 41471 (Pubitemid 37280975)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.42 , pp. 41462-41471
    • Horie, C.1    Suzuki, H.2    Sakaguchi, M.3    Mihara, K.4
  • 101
    • 67749095332 scopus 로고    scopus 로고
    • Hydrophobic profiles of the tail anchors in SLMAP dictate subcellular targeting
    • J.T. Byers, R.M. Guzzo, M. Salih, and B.S. Tuana Hydrophobic profiles of the tail anchors in SLMAP dictate subcellular targeting BMC Cell Biol. 10 2009 48
    • (2009) BMC Cell Biol. , vol.10 , pp. 48
    • Byers, J.T.1    Guzzo, R.M.2    Salih, M.3    Tuana, B.S.4
  • 102
    • 33746072623 scopus 로고    scopus 로고
    • Targeting of the tail-anchored peroxisomal membrane proteins PEX26 and PEX15 occurs through C-terminal PEX19-binding sites
    • DOI 10.1242/jcs.02979
    • A. Halbach, C. Landgraf, S. Lorenzen, K. Rosenkranz, R. Volkmer-Engert, R. Erdmann, and H. Rottensteiner Targeting of the tail-anchored peroxisomal membrane proteins PEX26 and PEX15 occurs through C-terminal PEX19-binding sites J. Cell Sci. 119 2006 2508 2517 (Pubitemid 44070432)
    • (2006) Journal of Cell Science , vol.119 , Issue.12 , pp. 2508-2517
    • Halbach, A.1    Landgraf, C.2    Lorenzen, S.3    Rosenkranz, K.4    Volkmer-Engert, R.5    Erdmann, R.6    Rottensteiner, H.7
  • 103
    • 34250183921 scopus 로고    scopus 로고
    • Post-translational integration of tail-anchored proteins is facilitated by defined molecular chaperones
    • DOI 10.1242/jcs.002410
    • B.M. Abell, C. Rabu, P. Leznicki, J.C. Young, and S. High Post-translational integration of tail-anchored proteins is facilitated by defined molecular chaperones J. Cell Sci. 120 2007 1743 1751 (Pubitemid 46930412)
    • (2007) Journal of Cell Science , vol.120 , Issue.10 , pp. 1743-1751
    • Abell, B.M.1    Rabu, C.2    Leznicki, P.3    Young, J.C.4    High, S.5
  • 105
    • 33947218544 scopus 로고    scopus 로고
    • Identification of a Targeting Factor for Posttranslational Membrane Protein Insertion into the ER
    • DOI 10.1016/j.cell.2007.01.036, PII S009286740700195X
    • S. Stefanovic, and R.S. Hegde Identification of a targeting factor for posttranslational membrane protein insertion into the ER Cell 128 2007 1147 1159 (Pubitemid 46427870)
    • (2007) Cell , vol.128 , Issue.6 , pp. 1147-1159
    • Stefanovic, S.1    Hegde, R.S.2
  • 106
    • 36849021602 scopus 로고    scopus 로고
    • Alternative function for the mitochondrial SAM complex in biogenesis of α-helical TOM proteins
    • DOI 10.1083/jcb.200706043
    • D. Stojanovski, B. Guiard, V. Kozjak-Pavlovic, N. Pfanner, and C. Meisinger Alternative function for the mitochondrial SAM complex in biogenesis of alpha-helical TOM proteins J. Cell Biol. 179 2007 881 893 (Pubitemid 350223486)
    • (2007) Journal of Cell Biology , vol.179 , Issue.5 , pp. 881-893
    • Stojanovski, D.1    Guiard, B.2    Kozjak-Pavlovic, V.3    Pfanner, N.4    Meisinger, C.5
  • 107
    • 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
    • DOI 10.1038/sj.cdd.4402055, PII 4402055
    • G. Bellot, P.F. Cartron, E. Er, L. Oliver, P. Juin, L.C. Armstrong, P. Bornstein, K. Mihara, S. Manon, and F.M. Vallette TOM22, a core component of the mitochondria outer membrane protein translocation pore, is a mitochondrial receptor for the proapoptotic protein Bax Cell Death Differ. 14 2007 785 794 (Pubitemid 46444516)
    • (2007) Cell Death and Differentiation , vol.14 , Issue.4 , pp. 785-794
    • Bellot, G.1    Cartron, P.-F.2    Er, E.3    Oliver, L.4    Juin, P.5    Armstrong, L.C.6    Bornstein, P.7    Mihara, K.8    Manon, S.9    Vallette, F.M.10
  • 109
    • 65249133454 scopus 로고    scopus 로고
    • TOM-independent complex formation of Bax and Bak in mammalian mitochondria during TNFalpha-induced apoptosis
    • K. Ross, T. Rudel, and V. Kozjak-Pavlovic TOM-independent complex formation of Bax and Bak in mammalian mitochondria during TNFalpha-induced apoptosis Cell Death Differ. 16 2009 697 707
    • (2009) Cell Death Differ. , vol.16 , pp. 697-707
    • Ross, K.1    Rudel, T.2    Kozjak-Pavlovic, V.3
  • 111
    • 0036977273 scopus 로고    scopus 로고
    • Bcl-2 and porin follow different pathways of TOM-dependent insertion into the mitochondrial outer membrane
    • DOI 10.1016/S0022-2836(02)00995-6
    • C. Motz, H. Martin, T. Krimmer, and J. Rassow Bcl-2 and porin follow different pathways of TOM-dependent insertion into the mitochondrial outer membrane J. Mol. Biol. 323 2002 729 738 (Pubitemid 36160226)
    • (2002) Journal of Molecular Biology , vol.323 , Issue.4 , pp. 729-738
    • Motz, C.1    Martin, H.2    Krimmer, T.3    Rassow, J.4
  • 112
    • 0028242493 scopus 로고
    • Assembly of Bcl-2 into microsomal and outer mitochondrial membranes
    • F. Janiak, B. Leber, and D.W. Andrews Assembly of Bcl-2 into microsomal and outer mitochondrial membranes J. Biol. Chem. 269 1994 9842 9849 (Pubitemid 24196593)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.13 , pp. 9842-9849
    • Janiak, F.1    Leber, B.2    Andrews, D.W.3
  • 113
    • 77950624268 scopus 로고    scopus 로고
    • Helix insertion into bilayers and the evolution of membrane proteins
    • R. Renthal Helix insertion into bilayers and the evolution of membrane proteins Cell. Mol. Life Sci. 67 2010 1077 1088
    • (2010) Cell. Mol. Life Sci. , vol.67 , pp. 1077-1088
    • Renthal, R.1
  • 114
    • 0037089084 scopus 로고    scopus 로고
    • Membrane topology and mitochondrial targeting of mitofusins, ubiquitous mammalian homologs of the transmembrane GTPase Fzo
    • M. Rojo, F. Legros, D. Chateau, and A. Lombes Membrane topology and mitochondrial targeting of mitofusins, ubiquitous mammalian homologs of the transmembrane GTPase Fzo J. Cell Sci. 2002 1663 1674 (Pubitemid 34520596)
    • (2002) Journal of Cell Science , vol.115 , Issue.8 , pp. 1663-1674
    • Rojo, M.1    Legros, F.2    Chateau, D.3    Lombes, A.4
  • 115
    • 38049016969 scopus 로고    scopus 로고
    • A novel insertion pathway of mitochondrial outer membrane proteins with multiple transmembrane segments
    • H. Otera, Y. Taira, C. Horie, Y. Suzuki, H. Suzuki, K. Setoguchi, H. Kato, T. Oka, and K. Mihara A novel insertion pathway of mitochondrial outer membrane proteins with multiple transmembrane segments J. Cell Biol. 179 2007 1355 1363
    • (2007) J. Cell Biol. , vol.179 , pp. 1355-1363
    • Otera, H.1    Taira, Y.2    Horie, C.3    Suzuki, Y.4    Suzuki, H.5    Setoguchi, K.6    Kato, H.7    Oka, T.8    Mihara, K.9
  • 116
    • 0032493625 scopus 로고    scopus 로고
    • Fzo1p is a mitochondrial outer membrane protein essential for the biogenesis of functional mitochondria in Saccharomyces cerevisiae
    • DOI 10.1074/jbc.273.32.20150
    • D. Rapaport, M. Brunner, W. Neupert, and B. Westermann Fzo1p is a mitochondrial outer membrane protein essential for the biogenesis of functional mitochondria in Saccharomyces cerevisiae J. Biol. Chem. 273 1998 20150 20155 (Pubitemid 28377572)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.32 , pp. 20150-20155
    • Rapaport, D.1    Brunner, M.2    Neupert, W.3    Westermann, B.4
  • 117
    • 0037428164 scopus 로고    scopus 로고
    • Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70
    • DOI 10.1016/S0092-8674(02)01250-3
    • J.C. Young, N.J. Hoogenraad, and F.-U. Hartl Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70 Cell 112 2003 41 50 (Pubitemid 36106417)
    • (2003) Cell , vol.112 , Issue.1 , pp. 41-50
    • Young, J.C.1    Hoogenraad, N.J.2    Hartl, F.U.3
  • 118
    • 0346687594 scopus 로고    scopus 로고
    • 3C motif
    • DOI 10.1016/j.tibs.2003.11.003
    • C.M. Koehler The small Tim proteins and the twin Cx3C motif Trends Biochem. Sci. 29 2004 1 4 (Pubitemid 38068471)
    • (2004) Trends in Biochemical Sciences , vol.29 , Issue.1 , pp. 1-4
    • Koehler, C.M.1


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