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Volumn 7, Issue 12, 2012, Pages

Reconstitution of Mitochondria Derived Vesicle Formation Demonstrates Selective Enrichment of Oxidized Cargo

Author keywords

[No Author keywords available]

Indexed keywords

MITOCHONDRIAL COMPLEX V; MITOCHONDRIAL ENZYME; OXIDIZED PROTEIN; PROTEIN DERIVATIVE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); UNCLASSIFIED DRUG;

EID: 84871537265     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0052830     Document Type: Article
Times cited : (246)

References (37)
  • 1
    • 0037009120 scopus 로고    scopus 로고
    • Membrane protein degradation by AAA proteases in mitochondria
    • Arnold I, Langer T, (2002) Membrane protein degradation by AAA proteases in mitochondria. Biochim Biophys Acta 1592: 89-96.
    • (2002) Biochim Biophys Acta , vol.1592 , pp. 89-96
    • Arnold, I.1    Langer, T.2
  • 2
    • 13244298414 scopus 로고    scopus 로고
    • Characterization of peptides released from mitochondria: evidence for constant proteolysis and peptide efflux
    • Augustin S, Nolden M, Muller S, Hardt O, Arnold I, et al. (2005) Characterization of peptides released from mitochondria: evidence for constant proteolysis and peptide efflux. J Biol Chem 280: 2691-2699.
    • (2005) J Biol Chem , vol.280 , pp. 2691-2699
    • Augustin, S.1    Nolden, M.2    Muller, S.3    Hardt, O.4    Arnold, I.5
  • 3
    • 0036713692 scopus 로고    scopus 로고
    • Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism
    • Bota DA, Davies KJ, (2002) Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism. Nat Cell Biol 4: 674-680.
    • (2002) Nat Cell Biol , vol.4 , pp. 674-680
    • Bota, D.A.1    Davies, K.J.2
  • 4
    • 38549110110 scopus 로고    scopus 로고
    • Fission and selective fusion govern mitochondrial segregation and elimination by autophagy
    • Twig G, Elorza A, Molina AJ, Mohamed H, Wikstrom JD, et al. (2008) Fission and selective fusion govern mitochondrial segregation and elimination by autophagy. Embo J 27: 433-446.
    • (2008) Embo J , vol.27 , pp. 433-446
    • Twig, G.1    Elorza, A.2    Molina, A.J.3    Mohamed, H.4    Wikstrom, J.D.5
  • 5
    • 76149140917 scopus 로고    scopus 로고
    • Regulation of OPA1 processing and mitochondrial fusion by m-AAA protease isoenzymes and OMA1
    • Ehses S, Raschke I, Mancuso G, Bernacchia A, Geimer S, et al. (2009) Regulation of OPA1 processing and mitochondrial fusion by m-AAA protease isoenzymes and OMA1. J Cell Biol 187: 1023-1036.
    • (2009) J Cell Biol , vol.187 , pp. 1023-1036
    • Ehses, S.1    Raschke, I.2    Mancuso, G.3    Bernacchia, A.4    Geimer, S.5
  • 6
    • 76149093590 scopus 로고    scopus 로고
    • Inducible proteolytic inactivation of OPA1 mediated by the OMA1 protease in mammalian cells
    • Head B, Griparic L, Amiri M, Gandre-Babbe S, van der Bliek AM, (2009) Inducible proteolytic inactivation of OPA1 mediated by the OMA1 protease in mammalian cells. J Cell Biol 187: 959-966.
    • (2009) J Cell Biol , vol.187 , pp. 959-966
    • Head, B.1    Griparic, L.2    Amiri, M.3    Gandre-Babbe, S.4    van der Bliek, A.M.5
  • 8
    • 67650348459 scopus 로고    scopus 로고
    • Frequency and selectivity of mitochondrial fusion are key to its quality maintenance function
    • Mouli PK, Twig G, Shirihai OS, (2009) Frequency and selectivity of mitochondrial fusion are key to its quality maintenance function. Biophys J 96: 3509-3518.
    • (2009) Biophys J , vol.96 , pp. 3509-3518
    • Mouli, P.K.1    Twig, G.2    Shirihai, O.S.3
  • 9
    • 79961239061 scopus 로고    scopus 로고
    • From the Cover: Impaired mitochondrial transport and Parkin-independent degeneration of respiratory chain-deficient dopamine neurons in vivo
    • Sterky FH, Lee S, Wibom R, Olson L, Larsson NG, (2011) From the Cover: Impaired mitochondrial transport and Parkin-independent degeneration of respiratory chain-deficient dopamine neurons in vivo. Proc Natl Acad Sci U S A 108: 12937-12942.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 12937-12942
    • Sterky, F.H.1    Lee, S.2    Wibom, R.3    Olson, L.4    Larsson, N.G.5
  • 10
    • 84856951239 scopus 로고    scopus 로고
    • Mitochondrial autophagy in cells with mtDNA mutations results from synergistic loss of transmembrane potential and mTORC1 inhibition
    • Gilkerson RW, De Vries RL, Lebot P, Wikstrom JD, Torgyekes E, et al. (2012) Mitochondrial autophagy in cells with mtDNA mutations results from synergistic loss of transmembrane potential and mTORC1 inhibition. Hum Mol Genet 21: 978-990.
    • (2012) Hum Mol Genet , vol.21 , pp. 978-990
    • Gilkerson, R.W.1    De Vries, R.L.2    Lebot, P.3    Wikstrom, J.D.4    Torgyekes, E.5
  • 11
  • 12
    • 84858701257 scopus 로고    scopus 로고
    • Spatial Parkin Translocation and Degradation of Damaged Mitochondria via Mitophagy in Live Cortical Neurons
    • Cai Q, Zakaria HM, Simone A, Sheng ZH (2012) Spatial Parkin Translocation and Degradation of Damaged Mitochondria via Mitophagy in Live Cortical Neurons. Curr Biol.
    • (2012) Curr Biol
    • Cai, Q.1    Zakaria, H.M.2    Simone, A.3    Sheng, Z.H.4
  • 13
    • 79551603345 scopus 로고    scopus 로고
    • Bioenergetics of neurons inhibit the translocation response of Parkin following rapid mitochondrial depolarization
    • Van Laar VS, Arnold B, Cassady SJ, Chu CT, Burton EA, et al. (2011) Bioenergetics of neurons inhibit the translocation response of Parkin following rapid mitochondrial depolarization. Hum Mol Genet 20: 927-940.
    • (2011) Hum Mol Genet , vol.20 , pp. 927-940
    • Van Laar, V.S.1    Arnold, B.2    Cassady, S.J.3    Chu, C.T.4    Burton, E.A.5
  • 14
    • 26844454131 scopus 로고    scopus 로고
    • BH3-ligand regulates access of MCL-1 to its E3 ligase
    • Warr MR, Acoca S, Liu Z, Germain M, Watson M, et al. (2005) BH3-ligand regulates access of MCL-1 to its E3 ligase. FEBS Lett 579: 5603-5608.
    • (2005) FEBS Lett , vol.579 , pp. 5603-5608
    • Warr, M.R.1    Acoca, S.2    Liu, Z.3    Germain, M.4    Watson, M.5
  • 15
    • 21244472965 scopus 로고    scopus 로고
    • Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis
    • Zhong Q, Gao W, Du F, Wang X, (2005) Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis. Cell 121: 1085-1095.
    • (2005) Cell , vol.121 , pp. 1085-1095
    • Zhong, Q.1    Gao, W.2    Du, F.3    Wang, X.4
  • 16
    • 21444442598 scopus 로고    scopus 로고
    • Instability of the mitofusin Fzo1 regulates mitochondrial morphology during the mating response of the yeast Saccharomyces cerevisiae
    • Neutzner A, Youle RJ, (2005) Instability of the mitofusin Fzo1 regulates mitochondrial morphology during the mating response of the yeast Saccharomyces cerevisiae. J Biol Chem 280: 18598-18603.
    • (2005) J Biol Chem , vol.280 , pp. 18598-18603
    • Neutzner, A.1    Youle, R.J.2
  • 17
    • 76649093912 scopus 로고    scopus 로고
    • Degradation of an intramitochondrial protein by the cytosolic proteasome
    • Azzu V, Brand MD, (2010) Degradation of an intramitochondrial protein by the cytosolic proteasome. J Cell Sci 123: 578-585.
    • (2010) J Cell Sci , vol.123 , pp. 578-585
    • Azzu, V.1    Brand, M.D.2
  • 18
    • 78649463381 scopus 로고    scopus 로고
    • Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkin-dependent manner upon induction of mitophagy
    • Gegg ME, Cooper JM, Chau KY, Rojo M, Schapira AH, et al. (2010) Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkin-dependent manner upon induction of mitophagy. Hum Mol Genet 19: 4861-4870.
    • (2010) Hum Mol Genet , vol.19 , pp. 4861-4870
    • Gegg, M.E.1    Cooper, J.M.2    Chau, K.Y.3    Rojo, M.4    Schapira, A.H.5
  • 19
    • 77955844260 scopus 로고    scopus 로고
    • The mitochondrial fusion-promoting factor mitofusin is a substrate of the PINK1/parkin pathway
    • Poole AC, Thomas RE, Yu S, Vincow ES, Pallanck L, (2010) The mitochondrial fusion-promoting factor mitofusin is a substrate of the PINK1/parkin pathway. PLoS One 5: e10054.
    • (2010) PLoS One , vol.5
    • Poole, A.C.1    Thomas, R.E.2    Yu, S.3    Vincow, E.S.4    Pallanck, L.5
  • 20
    • 77950384477 scopus 로고    scopus 로고
    • Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin
    • Ziviani E, Tao RN, Whitworth AJ, (2010) Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin. Proc Natl Acad Sci U S A 107: 5018-5023.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 5018-5023
    • Ziviani, E.1    Tao, R.N.2    Whitworth, A.J.3
  • 21
    • 78650729600 scopus 로고    scopus 로고
    • Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin
    • Tanaka A, Cleland MM, Xu S, Narendra DP, Suen DF, et al. (2010) Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin. J Cell Biol 191: 1367-1380.
    • (2010) J Cell Biol , vol.191 , pp. 1367-1380
    • Tanaka, A.1    Cleland, M.M.2    Xu, S.3    Narendra, D.P.4    Suen, D.F.5
  • 22
    • 79954520907 scopus 로고    scopus 로고
    • Broad activation of the ubiquitin-proteasome system by Parkin is critical for mitophagy
    • Chan NC, Salazar AM, Pham AH, Sweredoski MJ, Kolawa NJ, et al. (2011) Broad activation of the ubiquitin-proteasome system by Parkin is critical for mitophagy. Hum Mol Genet 20: 1726-1737.
    • (2011) Hum Mol Genet , vol.20 , pp. 1726-1737
    • Chan, N.C.1    Salazar, A.M.2    Pham, A.H.3    Sweredoski, M.J.4    Kolawa, N.J.5
  • 23
    • 38449107710 scopus 로고    scopus 로고
    • Outer mitochondrial membrane protein degradation by the proteasome
    • discussion 14-20
    • Neutzner A, Youle RJ, Karbowski M (2007) Outer mitochondrial membrane protein degradation by the proteasome. Novartis Found Symp 287: 4-14; discussion 14-20.
    • (2007) Novartis Found Symp , vol.287 , pp. 4-14
    • Neutzner, A.1    Youle, R.J.2    Karbowski, M.3
  • 24
    • 67949111205 scopus 로고    scopus 로고
    • Mitochondrial vesicles: an ancient process providing new links to peroxisomes
    • Andrade-Navarro MA, Sanchez-Pulido L, McBride HM, (2009) Mitochondrial vesicles: an ancient process providing new links to peroxisomes. Curr Opin Cell Biol 21: 560-567.
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 560-567
    • Andrade-Navarro, M.A.1    Sanchez-Pulido, L.2    McBride, H.M.3
  • 25
    • 38349023008 scopus 로고    scopus 로고
    • Cargo-selected transport from the mitochondria to peroxisomes is mediated by vesicular carriers
    • Neuspiel M, Schauss AC, Braschi E, Zunino R, Rippstein P, et al. (2008) Cargo-selected transport from the mitochondria to peroxisomes is mediated by vesicular carriers. Curr Biol 18: 102-108.
    • (2008) Curr Biol , vol.18 , pp. 102-108
    • Neuspiel, M.1    Schauss, A.C.2    Braschi, E.3    Zunino, R.4    Rippstein, P.5
  • 26
    • 78049529676 scopus 로고    scopus 로고
    • Vps35 mediates vesicle transport between the mitochondria and peroxisomes
    • Braschi E, Goyon V, Zunino R, Mohanty A, Xu L, et al. (2010) Vps35 mediates vesicle transport between the mitochondria and peroxisomes. Curr Biol 20: 1310-1315.
    • (2010) Curr Biol , vol.20 , pp. 1310-1315
    • Braschi, E.1    Goyon, V.2    Zunino, R.3    Mohanty, A.4    Xu, L.5
  • 27
    • 84856221632 scopus 로고    scopus 로고
    • A vesicular transport pathway shuttles cargo from mitochondria to lysosomes
    • Soubannier V, McLelland GL, Zunino R, Braschi E, Rippstein P, et al. (2012) A vesicular transport pathway shuttles cargo from mitochondria to lysosomes. Curr Biol 22: 135-141.
    • (2012) Curr Biol , vol.22 , pp. 135-141
    • Soubannier, V.1    McLelland, G.L.2    Zunino, R.3    Braschi, E.4    Rippstein, P.5
  • 28
    • 34548495323 scopus 로고    scopus 로고
    • The mitochondrial transcription factor TFAM coordinates the assembly of multiple DNA molecules into nucleoid-like structures
    • Kaufman BA, Durisic N, Mativetsky JM, Costantino S, Hancock MA, et al. (2007) The mitochondrial transcription factor TFAM coordinates the assembly of multiple DNA molecules into nucleoid-like structures. Mol Biol Cell 18: 3225-3236.
    • (2007) Mol Biol Cell , vol.18 , pp. 3225-3236
    • Kaufman, B.A.1    Durisic, N.2    Mativetsky, J.M.3    Costantino, S.4    Hancock, M.A.5
  • 29
    • 0027049521 scopus 로고
    • A signal-anchor sequence selective for the mitochondrial outer membrane
    • McBride HM, Millar DG, Li JM, Shore GC, (1992) A signal-anchor sequence selective for the mitochondrial outer membrane. J Cell Biol 119: 1451-1457.
    • (1992) J Cell Biol , vol.119 , pp. 1451-1457
    • McBride, H.M.1    Millar, D.G.2    Li, J.M.3    Shore, G.C.4
  • 30
    • 8944248278 scopus 로고    scopus 로고
    • The human mitochondrial import receptor, hTom20p, prevents a cryptic matrix targeting sequence from gaining access to the protein translocation machinery
    • McBride HM, Goping IS, Shore GC, (1996) The human mitochondrial import receptor, hTom20p, prevents a cryptic matrix targeting sequence from gaining access to the protein translocation machinery. J Cell Biol 134: 307-313.
    • (1996) J Cell Biol , vol.134 , pp. 307-313
    • McBride, H.M.1    Goping, I.S.2    Shore, G.C.3
  • 31
    • 0024299523 scopus 로고
    • Reconstitution of SEC gene product-dependent intercompartmental protein transport
    • Baker D, Hicke L, Rexach M, Schleyer M, Schekman R, (1988) Reconstitution of SEC gene product-dependent intercompartmental protein transport. Cell 54: 335-344.
    • (1988) Cell , vol.54 , pp. 335-344
    • Baker, D.1    Hicke, L.2    Rexach, M.3    Schleyer, M.4    Schekman, R.5
  • 32
    • 0025775567 scopus 로고
    • Distinct biochemical requirements for the budding, targeting, and fusion of ER-derived transport vesicles
    • Rexach MF, Schekman RW, (1991) Distinct biochemical requirements for the budding, targeting, and fusion of ER-derived transport vesicles. J Cell Biol 114: 219-229.
    • (1991) J Cell Biol , vol.114 , pp. 219-229
    • Rexach, M.F.1    Schekman, R.W.2
  • 33
    • 0021099569 scopus 로고
    • Membrane and cytosolic components affecting transport of the precursor for ornithine carbamyltransferase into mitochondria
    • Argan C, Lusty CJ, Shore GC, (1983) Membrane and cytosolic components affecting transport of the precursor for ornithine carbamyltransferase into mitochondria. J Biol Chem 258: 6667-6670.
    • (1983) J Biol Chem , vol.258 , pp. 6667-6670
    • Argan, C.1    Lusty, C.J.2    Shore, G.C.3
  • 35
    • 0032551769 scopus 로고    scopus 로고
    • Induction of the mitochondrial permeability transition by N-ethylmaleimide depends on secondary oxidation of critical thiol groups. Potentiation by copper-ortho-phenanthroline without dimerization of the adenine nucleotide translocase
    • Costantini P, Colonna R, Bernardi P, (1998) Induction of the mitochondrial permeability transition by N-ethylmaleimide depends on secondary oxidation of critical thiol groups. Potentiation by copper-ortho-phenanthroline without dimerization of the adenine nucleotide translocase. Biochim Biophys Acta 1365: 385-392.
    • (1998) Biochim Biophys Acta , vol.1365 , pp. 385-392
    • Costantini, P.1    Colonna, R.2    Bernardi, P.3
  • 36
    • 0027291429 scopus 로고
    • Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins from the cytosol
    • Orcl L, Palmer DJ, Amherdt M, Rothman JE, (1993) Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins from the cytosol. Nature 364: 732-734.
    • (1993) Nature , vol.364 , pp. 732-734
    • Orcl, L.1    Palmer, D.J.2    Amherdt, M.3    Rothman, J.E.4
  • 37
    • 0027724473 scopus 로고
    • Hydrolysis of bound GTP by ARF protein triggers uncoating of Golgi-derived COP-coated vesicles
    • Tanigawa G, Orci L, Amherdt M, Ravazzola M, Helms JB, et al. (1993) Hydrolysis of bound GTP by ARF protein triggers uncoating of Golgi-derived COP-coated vesicles. J Cell Biol 123: 1365-1371.
    • (1993) J Cell Biol , vol.123 , pp. 1365-1371
    • Tanigawa, G.1    Orci, L.2    Amherdt, M.3    Ravazzola, M.4    Helms, J.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.