메뉴 건너뛰기




Volumn 424, Issue 5, 2012, Pages 227-239

Impaired folding of the mitochondrial small TIM chaperones induces clearance by the i-AAA protease

Author keywords

disulfide bond; intermembrane space; MIA; mitochondria; Yme1

Indexed keywords

CHAPERONE; CYSTEINE; I ATPASES ASSOCIATED WITH DIVERSE CELLULAR ACTIVITIES PROTEASE; PROTEINASE; SMALL TRANSLOCASE OF THE INNER MEMBRANE10 CHAPERONE; SMALL TRANSLOCASE OF THE INNER MEMBRANE9 CHAPERONE; UNCLASSIFIED DRUG;

EID: 84869229480     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2012.09.019     Document Type: Article
Times cited : (52)

References (41)
  • 1
    • 33746575844 scopus 로고    scopus 로고
    • Evolution of the molecular machines for protein import into mitochondria
    • P. Dolezal, V. Likic, J. Tachezy, and T. Lithgow Evolution of the molecular machines for protein import into mitochondria Science 313 2006 314 318
    • (2006) Science , vol.313 , pp. 314-318
    • Dolezal, P.1    Likic, V.2    Tachezy, J.3    Lithgow, T.4
  • 3
    • 34249873947 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • W. Neupert, and J.M. Herrmann Translocation of proteins into mitochondria Annu. Rev. Biochem. 76 2007 723 749
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 723-749
    • Neupert, W.1    Herrmann, J.M.2
  • 6
    • 34848823742 scopus 로고    scopus 로고
    • Mitochondrial protein-import machinery: Correlating structure with function
    • M.J. Baker, A.E. Frazier, J.M. Gulbis, and M.T. Ryan Mitochondrial protein-import machinery: correlating structure with function Trends Cell Biol. 17 2007 456 464
    • (2007) Trends Cell Biol. , vol.17 , pp. 456-464
    • Baker, M.J.1    Frazier, A.E.2    Gulbis, J.M.3    Ryan, M.T.4
  • 7
    • 7544219638 scopus 로고    scopus 로고
    • New developments in mitochondrial assembly
    • C.M. Koehler New developments in mitochondrial assembly Annu. Rev. Cell Dev. Biol. 20 2004 309 335
    • (2004) Annu. Rev. Cell Dev. Biol. , vol.20 , pp. 309-335
    • Koehler, C.M.1
  • 8
    • 29544436323 scopus 로고    scopus 로고
    • Crystal structure of the mitochondrial chaperone TIM9.10 reveals a six-bladed alpha-propeller
    • C.T. Webb, M.A. Gorman, M. Lazarou, M.T. Ryan, and J.M. Gulbis Crystal structure of the mitochondrial chaperone TIM9.10 reveals a six-bladed alpha-propeller Mol. Cell 21 2006 123 133
    • (2006) Mol. Cell , vol.21 , pp. 123-133
    • Webb, C.T.1    Gorman, M.A.2    Lazarou, M.3    Ryan, M.T.4    Gulbis, J.M.5
  • 9
    • 64049101797 scopus 로고    scopus 로고
    • Structural and functional requirements for activity of the Tim9-Tim10 complex in mitochondrial protein import
    • M.J. Baker, C.T. Webb, D.A. Stroud, C.S. Palmer, A.E. Frazier, and B. Guiard Structural and functional requirements for activity of the Tim9-Tim10 complex in mitochondrial protein import Mol. Biol. Cell 20 2009 769 779
    • (2009) Mol. Biol. Cell , vol.20 , pp. 769-779
    • Baker, M.J.1    Webb, C.T.2    Stroud, D.A.3    Palmer, C.S.4    Frazier, A.E.5    Guiard, B.6
  • 10
    • 51349138652 scopus 로고    scopus 로고
    • The Tim8-Tim13 complex has multiple substrate binding sites and binds cooperatively to Tim23
    • K.N. Beverly, M.R. Sawaya, E. Schmid, and C.M. Koehler The Tim8-Tim13 complex has multiple substrate binding sites and binds cooperatively to Tim23 J. Mol. Biol. 382 2008 1144 1156
    • (2008) J. Mol. Biol. , vol.382 , pp. 1144-1156
    • Beverly, K.N.1    Sawaya, M.R.2    Schmid, E.3    Koehler, C.M.4
  • 11
    • 0032536045 scopus 로고    scopus 로고
    • Import of mitochondrial carriers mediated by essential proteins of the intermembrane space
    • C.M. Koehler, E. Jarosch, K. Tokatlidis, K. Schmid, R.J. Schweyen, and G. Schatz Import of mitochondrial carriers mediated by essential proteins of the intermembrane space Science 279 1998 369 373
    • (1998) Science , vol.279 , pp. 369-373
    • Koehler, C.M.1    Jarosch, E.2    Tokatlidis, K.3    Schmid, K.4    Schweyen, R.J.5    Schatz, G.6
  • 12
    • 0029827853 scopus 로고    scopus 로고
    • Import of carrier proteins into the mitochondrial inner membrane mediated by Tim22
    • C. Sirrenberg, M.F. Bauer, B. Guiard, W. Neupert, and M. Brunner Import of carrier proteins into the mitochondrial inner membrane mediated by Tim22 Nature 384 1996 582 585
    • (1996) Nature , vol.384 , pp. 582-585
    • Sirrenberg, C.1    Bauer, M.F.2    Guiard, B.3    Neupert, W.4    Brunner, M.5
  • 13
    • 0141643287 scopus 로고    scopus 로고
    • Juxtaposition of the two distal CX3C motifs via intrachain disulfide bonding is essential for the folding of Tim10
    • S. Allen, H. Lu, D. Thornton, and K. Tokatlidis Juxtaposition of the two distal CX3C motifs via intrachain disulfide bonding is essential for the folding of Tim10 J. Biol. Chem. 278 2003 38505 38513
    • (2003) J. Biol. Chem. , vol.278 , pp. 38505-38513
    • Allen, S.1    Lu, H.2    Thornton, D.3    Tokatlidis, K.4
  • 14
    • 84861329438 scopus 로고    scopus 로고
    • The MIA pathway: A tight bond between protein transport and oxidative folding in mitochondria
    • D. Stojanovski, P. Bragoszewski, and A. Chacinska The MIA pathway: a tight bond between protein transport and oxidative folding in mitochondria Biochim. Biophys. Acta 1823 2012 1142 1150
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 1142-1150
    • Stojanovski, D.1    Bragoszewski, P.2    Chacinska, A.3
  • 15
    • 84856853161 scopus 로고    scopus 로고
    • The mitochondrial disulfide relay: Redox-regulated protein import into the intermembrane space
    • J.M. Herrmann, and J. Riemer The mitochondrial disulfide relay: redox-regulated protein import into the intermembrane space J. Biol. Chem. 287 2011 4426 4433
    • (2011) J. Biol. Chem. , vol.287 , pp. 4426-4433
    • Herrmann, J.M.1    Riemer, J.2
  • 16
    • 41449099521 scopus 로고    scopus 로고
    • The Erv1-Mia40 disulfide relay system in the intermembrane space of mitochondria
    • K. Hell The Erv1-Mia40 disulfide relay system in the intermembrane space of mitochondria Biochim. Biophys. Acta 1783 2008 601 609
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 601-609
    • Hell, K.1
  • 18
    • 21244445718 scopus 로고    scopus 로고
    • A disulfide relay system in the intermembrane space of mitochondria that mediates protein import
    • N. Mesecke, N. Terziyska, C. Kozany, F. Baumann, W. Neupert, K. Hell, and J.M. Herrmann A disulfide relay system in the intermembrane space of mitochondria that mediates protein import Cell 121 2005 1059 1069
    • (2005) Cell , vol.121 , pp. 1059-1069
    • Mesecke, N.1    Terziyska, N.2    Kozany, C.3    Baumann, F.4    Neupert, W.5    Hell, K.6    Herrmann, J.M.7
  • 19
    • 9144273327 scopus 로고    scopus 로고
    • Identification of Tim40 that mediates protein sorting to the mitochondrial intermembrane space
    • M. Naoé, Y. Ohwa, D. Ishikawa, C. Ohshima, S. Nishikawa, H. Yamamoto, and T. Endo Identification of Tim40 that mediates protein sorting to the mitochondrial intermembrane space J. Biol. Chem. 279 2004 47815 47821
    • (2004) J. Biol. Chem. , vol.279 , pp. 47815-47821
    • Naoé, M.1    Ohwa, Y.2    Ishikawa, D.3    Ohshima, C.4    Nishikawa, S.5    Yamamoto, H.6    Endo, T.7
  • 20
    • 34547929482 scopus 로고    scopus 로고
    • Biogenesis of the essential Tim9-Tim10 chaperone complex of mitochondria: Site-specific recognition of cysteine residues by the intermembrane space receptor Mia40
    • D. Milenkovic, K. Gabriel, B. Guiard, A. Schulze-Specking, N. Pfanner, and A. Chacinska Biogenesis of the essential Tim9-Tim10 chaperone complex of mitochondria: site-specific recognition of cysteine residues by the intermembrane space receptor Mia40 J. Biol. Chem. 282 2007 22472 22480
    • (2007) J. Biol. Chem. , vol.282 , pp. 22472-22480
    • Milenkovic, D.1    Gabriel, K.2    Guiard, B.3    Schulze-Specking, A.4    Pfanner, N.5    Chacinska, A.6
  • 21
    • 34547896606 scopus 로고    scopus 로고
    • Oxidative folding of small Tims is mediated by site-specific docking onto Mia40 in the mitochondrial intermembrane space
    • D.P. Sideris, and K. Tokatlidis Oxidative folding of small Tims is mediated by site-specific docking onto Mia40 in the mitochondrial intermembrane space Mol. Microbiol. 65 2007 1360 1373
    • (2007) Mol. Microbiol. , vol.65 , pp. 1360-1373
    • Sideris, D.P.1    Tokatlidis, K.2
  • 22
    • 0040610684 scopus 로고    scopus 로고
    • Functional staging of ADP/ATP carrier translocation across the outer mitochondrial membrane
    • M.T. Ryan, H. Müller, and N. Pfanner Functional staging of ADP/ATP carrier translocation across the outer mitochondrial membrane J. Biol. Chem. 274 1999 20619 20627
    • (1999) J. Biol. Chem. , vol.274 , pp. 20619-20627
    • Ryan, M.T.1    Müller, H.2    Pfanner, N.3
  • 23
    • 0035283084 scopus 로고    scopus 로고
    • The three modules of ADP/ATP carrier cooperate in receptor recruitment and translocation into mitochondria
    • N. Wiedemann, N. Pfanner, and M.T. Ryan The three modules of ADP/ATP carrier cooperate in receptor recruitment and translocation into mitochondria EMBO J. 20 2001 951 960
    • (2001) EMBO J. , vol.20 , pp. 951-960
    • Wiedemann, N.1    Pfanner, N.2    Ryan, M.T.3
  • 24
    • 1842478040 scopus 로고    scopus 로고
    • The Tim8-Tim13 complex of Neurospora crassa functions in the assembly of proteins into both mitochondrial membranes
    • 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
    • (2004) J. Biol. Chem. , vol.279 , pp. 12396-12405
    • Hoppins, S.C.1    Nargang, F.E.2
  • 25
    • 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
    • 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
    • (2004) J. Biol. Chem. , vol.279 , pp. 18188-18194
    • Wiedemann, N.1    Truscott, K.N.2    Pfannschmidt, S.3    Guiard, B.4    Meisinger, C.5    Pfanner, N.6
  • 27
  • 28
    • 34250369119 scopus 로고    scopus 로고
    • Protein degradation within mitochondria: Versatile activities of AAA proteases and other peptidases
    • M. Koppen, and T. Langer Protein degradation within mitochondria: versatile activities of AAA proteases and other peptidases Crit. Rev. Biochem. Mol. Biol. 42 2007 221 242
    • (2007) Crit. Rev. Biochem. Mol. Biol. , vol.42 , pp. 221-242
    • Koppen, M.1    Langer, T.2
  • 30
    • 71749117953 scopus 로고    scopus 로고
    • AAA proteases in mitochondria: Diverse functions of membrane-bound proteolytic machines
    • T. Tatsuta, and T. Langer AAA proteases in mitochondria: diverse functions of membrane-bound proteolytic machines Res. Microbiol. 160 2009 711 717
    • (2009) Res. Microbiol. , vol.160 , pp. 711-717
    • Tatsuta, T.1    Langer, T.2
  • 31
    • 75349107775 scopus 로고    scopus 로고
    • Diverse functions of mitochondrial AAA + proteins: Protein activation, disaggregation, and degradation
    • K.N. Truscott, B.R. Lowth, P.R. Strack, and D.A. Dougan Diverse functions of mitochondrial AAA + proteins: protein activation, disaggregation, and degradation Biochem. Cell Biol. 88 2010 97 108
    • (2010) Biochem. Cell Biol. , vol.88 , pp. 97-108
    • Truscott, K.N.1    Lowth, B.R.2    Strack, P.R.3    Dougan, D.A.4
  • 32
    • 0033602381 scopus 로고    scopus 로고
    • Chaperone-like activity of the AAA domain of the yeast Yme1 AAA protease
    • K. Leonhard, A. Stiegler, W. Neupert, and T. Langer Chaperone-like activity of the AAA domain of the yeast Yme1 AAA protease Nature 398 1999 348 351
    • (1999) Nature , vol.398 , pp. 348-351
    • Leonhard, K.1    Stiegler, A.2    Neupert, W.3    Langer, T.4
  • 34
    • 76149084543 scopus 로고    scopus 로고
    • A novel intermembrane space-targeting signal docks cysteines onto Mia40 during mitochondrial oxidative folding
    • D.P. Sideris, N. Petrakis, N. Katrakili, D. Mikropoulou, A. Gallo, and S. Ciofi-Baffoni A novel intermembrane space-targeting signal docks cysteines onto Mia40 during mitochondrial oxidative folding J. Cell Biol. 187 2009 1007 1022
    • (2009) J. Cell Biol. , vol.187 , pp. 1007-1022
    • Sideris, D.P.1    Petrakis, N.2    Katrakili, N.3    Mikropoulou, D.4    Gallo, A.5    Ciofi-Baffoni, S.6
  • 35
    • 38749148392 scopus 로고    scopus 로고
    • Precursor oxidation by Mia40 and Erv1 promotes vectorial transport of proteins into the mitochondrial intermembrane space
    • J.M. Müller, D. Milenkovic, B. Guiard, N. Pfanner, and A. Chacinska Precursor oxidation by Mia40 and Erv1 promotes vectorial transport of proteins into the mitochondrial intermembrane space Mol. Biol. Cell 19 2008 226 236
    • (2008) Mol. Biol. Cell , vol.19 , pp. 226-236
    • Müller, J.M.1    Milenkovic, D.2    Guiard, B.3    Pfanner, N.4    Chacinska, A.5
  • 37
    • 0033639076 scopus 로고    scopus 로고
    • Membrane protein degradation by AAA proteases in mitochondria: Extraction of substrates from either membrane surface
    • K. Leonhard, B. Guiard, G. Pellecchia, A. Tzagoloff, W. Neupert, and T. Langer Membrane protein degradation by AAA proteases in mitochondria: extraction of substrates from either membrane surface Mol. Cell 5 2000 629 638
    • (2000) Mol. Cell , vol.5 , pp. 629-638
    • Leonhard, K.1    Guiard, B.2    Pellecchia, G.3    Tzagoloff, A.4    Neupert, W.5    Langer, T.6
  • 38
    • 77956391459 scopus 로고    scopus 로고
    • Regulation of mitochondrial phospholipids by Ups1/PRELI-like proteins depends on proteolysis and Mdm35
    • C. Potting, C. Wilmes, T. Engmann, C. Osman, and T. Langer Regulation of mitochondrial phospholipids by Ups1/PRELI-like proteins depends on proteolysis and Mdm35 EMBO J. 29 2010 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
  • 39
    • 0034039615 scopus 로고    scopus 로고
    • A de novo missense mutation in a critical domain of the X-linked DDP gene causes the typical deafness-dystonia-optic atrophy syndrome
    • L. Tranebjaerg, B.C. Hamel, F.J. Gabreels, W.O. Renier, and M. Van Ghelue A de novo missense mutation in a critical domain of the X-linked DDP gene causes the typical deafness-dystonia-optic atrophy syndrome Eur. J. Hum. Genet. 8 2000 464 467
    • (2000) Eur. J. Hum. Genet. , vol.8 , pp. 464-467
    • Tranebjaerg, L.1    Hamel, B.C.2    Gabreels, F.J.3    Renier, W.O.4    Van Ghelue, M.5
  • 40
    • 0000856498 scopus 로고
    • Two nuclear mutations that block mitochondrial protein import in yeast
    • M.P. Yaffe, and G. Schatz Two nuclear mutations that block mitochondrial protein import in yeast Proc. Natl Acad. Sci. USA 81 1984 4819 4823
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 4819-4823
    • Yaffe, M.P.1    Schatz, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.