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Volumn 524, Issue 7566, 2015, Pages 485-488

Mistargeted mitochondrial proteins activate a proteostatic response in the cytosol

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; MITOCHONDRIAL PROTEIN; PROTEIN PRECURSOR; PROTEOME; TRANSCRIPTOME; PROTEASOME; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 84940556804     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature14951     Document Type: Article
Times cited : (318)

References (53)
  • 1
    • 68749112707 scopus 로고    scopus 로고
    • Importing mitochondrial proteins: Machineries and mechanisms
    • Chacinska, A., Koehler, C. M., Milenkovic, D., Lithgow, T. & Pfanner, N. Importing mitochondrial proteins: machineries and mechanisms. Cell 138, 628-644 (2009).
    • (2009) Cell , vol.138 , pp. 628-644
    • Chacinska, A.1    Koehler, C.M.2    Milenkovic, D.3    Lithgow, T.4    Pfanner, N.5
  • 2
    • 79851512985 scopus 로고    scopus 로고
    • Structural insight into the mitochondrial protein import system
    • Endo, T., Yamano, K. & Kawano, S. Structural insight into the mitochondrial protein import system. Biochim. Biophys. Acta 1808, 955-970 (2011).
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 955-970
    • Endo, T.1    Yamano, K.2    Kawano, S.3
  • 3
    • 34249873947 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • Neupert, W. & Herrmann, J. M. Translocation of proteins into mitochondria. Annu. Rev. Biochem. 76, 723-749 (2007).
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 723-749
    • Neupert, W.1    Herrmann, J.M.2
  • 4
    • 77953020406 scopus 로고    scopus 로고
    • On the mechanism of preprotein import by the mitochondrial presequence translocase
    • van der Laan, M., Hutu, D. P. & Rehling, P. On the mechanism of preprotein import by the mitochondrial presequence translocase. Biochim. Biophys. Acta 1803, 732-739 (2010).
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 732-739
    • Van Der-Laan, M.1    Hutu, D.P.2    Rehling, P.3
  • 5
    • 20844457757 scopus 로고    scopus 로고
    • Essential role of Mia40 in import and assembly of mitochondrial intermembrane space proteins
    • Chacinska, A. et al. Essential role of Mia40 in import and assembly of mitochondrial intermembrane space proteins. EMBO J. 23, 3735-3746 (2004).
    • (2004) EMBO J. , vol.23 , pp. 3735-3746
    • Chacinska, A.1
  • 6
    • 55949134924 scopus 로고    scopus 로고
    • Mitochondrial protein import: Precursor oxidation in a ternary complex with disulfide carrier and sulfhydryl oxidase
    • Stojanovski, D. et al. Mitochondrial protein import: precursor oxidation in a ternary complex with disulfide carrier and sulfhydryl oxidase. J. Cell Biol. 183, 195-202 (2008).
    • (2008) J. Cell Biol. , vol.183 , pp. 195-202
    • Stojanovski, D.1
  • 7
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S. E. et al. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics 1, 376-386 (2002).
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1
  • 8
    • 84879001260 scopus 로고    scopus 로고
    • The ubiquitinproteasome systemregulates mitochondrial intermembrane space proteins
    • Bragoszewski, P., Gornicka, A., Sztolsztener, M. E. & Chacinska, A. The ubiquitinproteasome systemregulates mitochondrial intermembrane space proteins. Mol. Cell. Biol. 33, 2136-2148 (2013).
    • (2013) Mol. Cell. Biol. , vol.33 , pp. 2136-2148
    • Bragoszewski, P.1    Gornicka, A.2    Sztolsztener, M.E.3    Chacinska, A.4
  • 9
    • 84870907436 scopus 로고    scopus 로고
    • Cleaning up: ER-associated degradation to the rescue
    • Brodsky, J. L. Cleaning up: ER-associated degradation to the rescue. Cell 151, 1163-1167 (2012).
    • (2012) Cell , vol.151 , pp. 1163-1167
    • Brodsky, J.L.1
  • 10
    • 82755187338 scopus 로고    scopus 로고
    • Intracellular protein degradation: From a vague idea through the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting
    • Ciechanover, A. Intracellular protein degradation: from a vague idea through the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting. Biochim. Biophys. Acta 1824, 3-13 (2012).
    • (2012) Biochim. Biophys. Acta , vol.1824 , pp. 3-13
    • Ciechanover, A.1
  • 11
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • Finley, D. Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu. Rev. Biochem. 78, 477-513 (2009).
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 477-513
    • Finley, D.1
  • 12
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg, A. L. Protein degradation and protection against misfolded or damaged proteins. Nature 426, 895-899 (2003).
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 13
    • 84934890286 scopus 로고    scopus 로고
    • Retro-translocation of mitochondrial intermembrane space proteins
    • Bragoszewski, P. et al. Retro-translocation ofmitochondrial intermembrane space proteins. Proc. Natl Acad. Sci. USA 112, 7713-7718 (2015).
    • (2015) Proc. Natl Acad. Sci. USA , vol.112 , pp. 7713-7718
    • Bragoszewski, P.1
  • 15
    • 34547838178 scopus 로고    scopus 로고
    • 20S proteasome assembly is orchestrated by two distinct pairs of chaperones in yeast and in mammals
    • Le Tallec, B. et al. 20S proteasome assembly is orchestrated by two distinct pairs of chaperones in yeast and in mammals. Mol. Cell 27, 660-674 (2007).
    • (2007) Mol. Cell , vol.27 , pp. 660-674
    • Le Tallec, B.1
  • 16
    • 33845681479 scopus 로고    scopus 로고
    • Cooperation of multiple chaperones required for the assembly of mammalian 20S proteasomes
    • Hirano, Y. et al. Cooperation of multiple chaperones required for the assembly of mammalian 20S proteasomes. Mol. Cell 24, 977-984 (2006).
    • (2006) Mol. Cell , vol.24 , pp. 977-984
    • Hirano, Y.1
  • 17
    • 0032548998 scopus 로고    scopus 로고
    • Ump1p is required for proper maturation of the 20S proteasome and becomes its substrate upon completion of the assembly
    • Ramos, P.C., Hockendorff, J., Johnson, E. S., Varshavsky, A. & Dohmen, R. J. Ump1p is required for proper maturation of the 20S proteasome and becomes its substrate upon completion of the assembly. Cell 92, 489-499 (1998).
    • (1998) Cell , vol.92 , pp. 489-499
    • Ramos, P.C.1    Hockendorff, J.2    Johnson, E.S.3    Varshavsky, A.4    Dohmen, R.J.5
  • 18
    • 84906791334 scopus 로고    scopus 로고
    • An inducible chaperone adapts proteasome assembly to stress
    • Hanssum, A. et al. An inducible chaperone adapts proteasome assembly to stress. Mol. Cell 55, 566-577 (2014).
    • (2014) Mol. Cell , vol.55 , pp. 566-577
    • Hanssum, A.1
  • 19
    • 0034643336 scopus 로고    scopus 로고
    • Rapid degradation of a large fraction of newly synthesized proteins by proteasomes
    • Schubert, U. et al. Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature 404, 770-774 (2000).
    • (2000) Nature , vol.404 , pp. 770-774
    • Schubert, U.1
  • 20
    • 84880442209 scopus 로고    scopus 로고
    • Protein import and oxidative folding in the mitochondrial intermembrane space of intact mammalian cells
    • Fischer, M. et al. Protein import and oxidative folding in the mitochondrial intermembrane space of intact mammalian cells. Mol. Biol. Cell 24, 2160-2170 (2013).
    • (2013) Mol. Biol. Cell , vol.24 , pp. 2160-2170
    • Fischer, M.1
  • 21
    • 10744229056 scopus 로고    scopus 로고
    • Pam16has an essential role in the mitochondrial protein import motor
    • Frazier, A. E. et al. Pam16has an essential role in the mitochondrial protein import motor. Nature Struct. Mol. Biol. 11, 226-233 (2004).
    • (2004) Nature Struct. Mol. Biol. , vol.11 , pp. 226-233
    • Frazier, A.E.1
  • 22
    • 20244373481 scopus 로고    scopus 로고
    • Mitochondrial presequence translocase: Switching between TOM tethering and motor recruitment involves Tim21 and Tim17
    • Chacinska, A. et al. Mitochondrial presequence translocase: switching between TOM tethering and motor recruitment involves Tim21 and Tim17. Cell 120, 817-829 (2005).
    • (2005) Cell , vol.120 , pp. 817-829
    • Chacinska, A.1
  • 23
    • 13244258435 scopus 로고    scopus 로고
    • Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation
    • Bennett, E. J., Bence, N. F., Jayakumar, R. & Kopito, R. R. Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation. Mol. Cell 17, 351-365 (2005).
    • (2005) Mol. Cell , vol.17 , pp. 351-365
    • Bennett, E.J.1    Bence, N.F.2    Jayakumar, R.3    Kopito, R.R.4
  • 24
    • 84885095437 scopus 로고    scopus 로고
    • Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress
    • Escusa-Toret, S., Vonk, W. I. & Frydman, J. Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress. Nature Cell Biol. 15, 1231-1243 (2013).
    • (2013) Nature Cell Biol. , vol.15 , pp. 1231-1243
    • Escusa-Toret, S.1    Vonk, W.I.2    Frydman, J.3
  • 25
    • 78649728763 scopus 로고    scopus 로고
    • The mitochondrial UPR-protecting organelle protein homeostasis
    • Haynes, C. M. & Ron, D. The mitochondrial UPR-protecting organelle protein homeostasis. J. Cell Sci. 123, 3849-3855 (2010).
    • (2010) J. Cell Sci. , vol.123 , pp. 3849-3855
    • Haynes, C.M.1    Ron, D.2
  • 26
    • 0037009521 scopus 로고    scopus 로고
    • A mitochondrial specific stress response inmammalian cells
    • Zhao, Q. et al. A mitochondrial specific stress response inmammalian cells. EMBO J. 21, 4411-4419 (2002).
    • (2002) EMBO J. , vol.21 , pp. 4411-4419
    • Zhao, Q.1
  • 27
    • 84864744900 scopus 로고    scopus 로고
    • Mitochondrial import efficiency of ATFS-1 regulates mitochondrial UPR activation
    • Nargund, A. M., Pellegrino, M. W., Fiorese, C. J., Baker, B. M. & Haynes, C. M. Mitochondrial import efficiency of ATFS-1 regulates mitochondrial UPR activation. Science 337, 587-590 (2012).
    • (2012) Science , vol.337 , pp. 587-590
    • Nargund, A.M.1    Pellegrino, M.W.2    Fiorese, C.J.3    Baker, B.M.4    Haynes, C.M.5
  • 28
    • 84866182143 scopus 로고    scopus 로고
    • RPN-6 determines C. Elegans longevity under proteotoxic stress conditions
    • Vilchez, D. et al. RPN-6 determines C. elegans longevity under proteotoxic stress conditions. Nature 489, 263-268 (2012).
    • (2012) Nature , vol.489 , pp. 263-268
    • Vilchez, D.1
  • 29
    • 78650944949 scopus 로고    scopus 로고
    • The cell-non-autonomous nature of electron transport chain-mediated longevity
    • Durieux, J., Wolff, S. & Dillin, A. The cell-non-autonomous nature of electron transport chain-mediated longevity. Cell 144, 79-91 (2011).
    • (2011) Cell , vol.144 , pp. 79-91
    • Durieux, J.1    Wolff, S.2    Dillin, A.3
  • 30
    • 84878138385 scopus 로고    scopus 로고
    • Mitonuclear protein imbalance as a conserved longevity mechanism
    • Houtkooper, R. H. et al. Mitonuclear protein imbalance as a conserved longevity mechanism. Nature 497, 451-457 (2013).
    • (2013) Nature , vol.497 , pp. 451-457
    • Houtkooper, R.H.1
  • 31
    • 10744228445 scopus 로고    scopus 로고
    • A J-protein is an essential subunit of the presequence translocase-associated protein import motor of mitochondria
    • Truscott, K. N. et al. A J-protein is an essential subunit of the presequence translocase-associated protein import motor of mitochondria. J. Cell Biol. 163, 707-713 (2003).
    • (2003) J. Cell Biol. , vol.163 , pp. 707-713
    • Truscott, K.N.1
  • 32
    • 84867476990 scopus 로고    scopus 로고
    • In vivo evidence for cooperation of Mia40 and Erv1 in the oxidation of mitochondrial proteins
    • Böttinger, L. et al. In vivo evidence for cooperation of Mia40 and Erv1 in the oxidation of mitochondrial proteins. Mol. Biol. Cell 23, 3957-3969 (2012).
    • (2012) Mol. Biol. Cell , vol.23 , pp. 3957-3969
    • Böttinger, L.1
  • 33
    • 84897518469 scopus 로고    scopus 로고
    • Uniform nomenclature for the mitochondrial contact site and cristae organizing system
    • Pfanner, N. et al. Uniform nomenclature for the mitochondrial contact site and cristae organizing system. J. Cell Biol. 204, 1083-1086 (2014).
    • (2014) J. Cell Biol. , vol.204 , pp. 1083-1086
    • Pfanner, N.1
  • 34
    • 0023987428 scopus 로고
    • Point mutations destabilizing a precursor protein enhance its post-translational import into mitochondria
    • Vestweber, D. & Schatz, G. Point mutations destabilizing a precursor protein enhance its post-translational import into mitochondria. EMBO J. 7, 1147-1151 (1988).
    • (1988) EMBO J. , vol.7 , pp. 1147-1151
    • Vestweber, D.1    Schatz, G.2
  • 35
    • 84869221103 scopus 로고    scopus 로고
    • Role of the AAA protease Yme1 in folding of proteins in the intermembrane space of mitochondria
    • Schreiner, B. et al. Role of the AAA protease Yme1 in folding of proteins in the intermembrane space of mitochondria. Mol. Biol. Cell 23, 4335-4346 (2012).
    • (2012) Mol. Biol. Cell , vol.23 , pp. 4335-4346
    • Schreiner, B.1
  • 36
    • 84876996918 scopus 로고    scopus 로고
    • TopHat2: Accurate alignment of transcriptomes in the presence of insertions, deletions and gene fusions
    • Kim, D. et al. TopHat2: accurate alignment of transcriptomes in the presence of insertions, deletions and gene fusions. Genome Biol. 14, R36 (2013).
    • (2013) Genome Biol. , vol.14 , pp. R36
    • Kim, D.1
  • 37
    • 84859210032 scopus 로고    scopus 로고
    • Fast gapped-read alignment with Bowtie 2
    • Langmead, B. & Salzberg, S. L. Fast gapped-read alignment with Bowtie 2. Nature Methods 9, 357-359 (2012).
    • (2012) Nature Methods , vol.9 , pp. 357-359
    • Langmead, B.1    Salzberg, S.L.2
  • 38
    • 68549104404 scopus 로고    scopus 로고
    • The Sequence Alignment/Map format and SAMtools
    • Li, H. et al. The Sequence Alignment/Map format and SAMtools. Bioinformatics 25, 2078-2079 (2009).
    • (2009) Bioinformatics , vol.25 , pp. 2078-2079
    • Li, H.1
  • 39
    • 84905390734 scopus 로고    scopus 로고
    • The INA complex facilitates assembly of the peripheral stalk of the mitochondrial F1Fo-ATP synthase
    • Lytovchenko, O. et al. The INA complex facilitates assembly of the peripheral stalk of the mitochondrial F1Fo-ATP synthase. EMBO J. 33, 1624-1638 (2014).
    • (2014) EMBO J. , vol.33 , pp. 1624-1638
    • Lytovchenko, O.1
  • 40
    • 38349082663 scopus 로고    scopus 로고
    • Proteomics characterization of mouse kidney peroxisomes by tandem mass spectrometry and protein correlation profiling
    • Wiese, S. et al. Proteomics characterization of mouse kidney peroxisomes by tandem mass spectrometry and protein correlation profiling. Mol. Cell. Proteomics 6, 2045-2057 (2007).
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 2045-2057
    • Wiese, S.1
  • 41
    • 57449099865 scopus 로고    scopus 로고
    • Max Quant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox, J. & Mann, M. Max Quant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nature Biotechnol. 26, 1367-1372 (2008).
    • (2008) Nature Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 42
    • 79953701087 scopus 로고    scopus 로고
    • Andromeda: A peptide search engine integrated into the MaxQuant environment
    • Cox, J. et al. Andromeda: a peptide search engine integrated into the MaxQuant environment. J. Proteome Res. 10, 1794-1805 (2011).
    • (2011) J. Proteome Res. , vol.10 , pp. 1794-1805
    • Cox, J.1
  • 43
    • 84891796097 scopus 로고    scopus 로고
    • ProteomeXchange provides globally coordinated proteomics data submission and dissemination
    • Vizcaíno, J. A. et al. ProteomeXchange provides globally coordinated proteomics data submission and dissemination. Nature Biotechnol. 32, 223-226 (2014).
    • (2014) Nature Biotechnol. , vol.32 , pp. 223-226
    • Vizcaíno, J.A.1
  • 44
    • 84874762979 scopus 로고    scopus 로고
    • The PRoteomics IDEntifications (PRIDE) database and associated tools: Status in 2013
    • Vizcaíno, J. A. et al. The PRoteomics IDEntifications (PRIDE) database and associated tools: status in 2013. Nucleic Acids Res. 41, D1063-D1069 (2013).
    • (2013) Nucleic Acids Res. , vol.41 , pp. D1063-D1069
    • Vizcaíno, J.A.1
  • 45
    • 24044440971 scopus 로고    scopus 로고
    • BiNGO: A Cytoscape plugin to assess overrepresentation of gene ontology categories in biological networks
    • Maere, S., Heymans, K. & Kuiper, M. BiNGO: a Cytoscape plugin to assess overrepresentation of gene ontology categories in biological networks. Bioinformatics 21, 3448-3449 (2005).
    • (2005) Bioinformatics , vol.21 , pp. 3448-3449
    • Maere, S.1    Heymans, K.2    Kuiper, M.3
  • 46
    • 0242490780 scopus 로고    scopus 로고
    • Cytoscape: A software environment for integrated models of biomolecular interaction networks
    • Shannon, P. et al. Cytoscape: a software environment for integrated models of biomolecular interaction networks. Genome Res. 13, 2498-2504 (2003).
    • (2003) Genome Res. , vol.13 , pp. 2498-2504
    • Shannon, P.1
  • 47
    • 80053445278 scopus 로고    scopus 로고
    • Elevated proteasome capacity extends replicative lifespan in Saccharomyces cerevisiae
    • Kruegel, U. et al. Elevated proteasome capacity extends replicative lifespan in Saccharomyces cerevisiae. PLoS Genet. 7, e1002253 (2011).
    • (2011) PLoS Genet. , vol.7 , pp. e1002253
    • Kruegel, U.1
  • 49
    • 0023286894 scopus 로고
    • Fungal small nuclear ribonucleoproteins share properties with plant and vertebrate U-snRNPs
    • Tollervey, D. & Mattaj, I. W. Fungal small nuclear ribonucleoproteins share properties with plant and vertebrate U-snRNPs. EMBO J. 6, 469-476 (1987).
    • (1987) EMBO J. , vol.6 , pp. 469-476
    • Tollervey, D.1    Mattaj, I.W.2
  • 50
    • 0037129827 scopus 로고    scopus 로고
    • Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes
    • research0034
    • Vandesompele, J. et al. Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes. Genome Biol. 3, research0034 (2002).
    • (2002) Genome Biol. , vol.3
    • Vandesompele, J.1
  • 51
    • 70549086797 scopus 로고    scopus 로고
    • Validation of reference genes for quantitative expression analysis by real-time RT-PCR in Saccharomyces cerevisiae
    • Teste, M. A., Duquenne, M., Francois, J. M. & Parrou, J. L. Validation of reference genes for quantitative expression analysis by real-time RT-PCR in Saccharomyces cerevisiae. BMC Mol. Biol. 10, 99 (2009).
    • (2009) BMC Mol. Biol. , vol.10 , pp. 99
    • Teste, M.A.1    Duquenne, M.2    Francois, J.M.3    Parrou, J.L.4
  • 52
    • 84861850112 scopus 로고    scopus 로고
    • A novel strategy for selection and validation of reference genes in dynamic multidimensional experimental design in yeast
    • Cankorur-Cetinkaya, A. et al. A novel strategy for selection and validation of reference genes in dynamic multidimensional experimental design in yeast. PLoS ONE 7, e38351 (2012).
    • (2012) PLoS ONE , vol.7 , pp. e38351
    • Cankorur-Cetinkaya, A.1
  • 53
    • 0034733591 scopus 로고    scopus 로고
    • Rapid and reliable protein extraction from yeast
    • Kushnirov, V. V. Rapid and reliable protein extraction from yeast. Yeast 16, 857-860 (2000).
    • (2000) Yeast , vol.16 , pp. 857-860
    • Kushnirov, V.V.1


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