메뉴 건너뛰기




Volumn 63, Issue 1, 2016, Pages 21-33

Ubiquilins Chaperone and Triage Mitochondrial Membrane Proteins for Degradation

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CHAPERONE; LIGASE; MEMBRANE PROTEIN; MITOCHONDRIAL MEMBRANE PROTEIN; POLYGLUTAMINE; PROTEASOME; PROTEIN PRECURSOR; UBIQUILIN; UBIQUITIN; UNCLASSIFIED DRUG; CARRIER PROTEIN; CELL CYCLE PROTEIN; PEPTIDE; PROTEIN AGGREGATE; SYNJ2BP PROTEIN, HUMAN; UBIQUITIN PROTEIN LIGASE; UBQLN1 PROTEIN, HUMAN; UBQLN2 PROTEIN, HUMAN;

EID: 84988013632     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2016.05.020     Document Type: Article
Times cited : (188)

References (51)
  • 1
    • 67650915066 scopus 로고    scopus 로고
    • Selective processing and metabolism of disease-causing mutant prion proteins
    • Ashok, A., Hegde, R.S., Selective processing and metabolism of disease-causing mutant prion proteins. PLoS Pathog., 5, 2009, e1000479.
    • (2009) PLoS Pathog. , vol.5 , pp. e1000479
    • Ashok, A.1    Hegde, R.S.2
  • 2
    • 0024966540 scopus 로고
    • Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle
    • Bernstein, H.D., Poritz, M.A., Strub, K., Hoben, P.J., Brenner, S., Walter, P., Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle. Nature 340 (1989), 482–486.
    • (1989) Nature , vol.340 , pp. 482-486
    • Bernstein, H.D.1    Poritz, M.A.2    Strub, K.3    Hoben, P.J.4    Brenner, S.5    Walter, P.6
  • 3
    • 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 (2009), 628–644.
    • (2009) Cell , vol.138 , pp. 628-644
    • Chacinska, A.1    Koehler, C.M.2    Milenkovic, D.3    Lithgow, T.4    Pfanner, N.5
  • 4
    • 0037143649 scopus 로고    scopus 로고
    • Addition of a photocrosslinking amino acid to the genetic code of Escherichiacoli
    • Chin, J.W., Martin, A.B., King, D.S., Wang, L., Schultz, P.G., Addition of a photocrosslinking amino acid to the genetic code of Escherichiacoli. Proc. Natl. Acad. Sci. USA 99 (2002), 11020–11024.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11020-11024
    • Chin, J.W.1    Martin, A.B.2    King, D.S.3    Wang, L.4    Schultz, P.G.5
  • 8
    • 3342879140 scopus 로고    scopus 로고
    • Identification of ubiquitin-interacting proteins in purified polyglutamine aggregates
    • Doi, H., Mitsui, K., Kurosawa, M., Machida, Y., Kuroiwa, Y., Nukina, N., Identification of ubiquitin-interacting proteins in purified polyglutamine aggregates. FEBS Lett. 571 (2004), 171–176.
    • (2004) FEBS Lett. , vol.571 , pp. 171-176
    • Doi, H.1    Mitsui, K.2    Kurosawa, M.3    Machida, Y.4    Kuroiwa, Y.5    Nukina, N.6
  • 9
    • 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 (2009), 477–513.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 477-513
    • Finley, D.1
  • 10
    • 0037450802 scopus 로고    scopus 로고
    • Substrate-specific function of the translocon-associated protein complex during translocation across the ER membrane
    • Fons, R.D., Bogert, B.A., Hegde, R.S., Substrate-specific function of the translocon-associated protein complex during translocation across the ER membrane. J. Cell Biol. 160 (2003), 529–539.
    • (2003) J. Cell Biol. , vol.160 , pp. 529-539
    • Fons, R.D.1    Bogert, B.A.2    Hegde, R.S.3
  • 11
    • 34248180045 scopus 로고    scopus 로고
    • A conditional yeast E1 mutant blocks the ubiquitin-proteasome pathway and reveals a role for ubiquitin conjugates in targeting Rad23 to the proteasome
    • Ghaboosi, N., Deshaies, R.J., A conditional yeast E1 mutant blocks the ubiquitin-proteasome pathway and reveals a role for ubiquitin conjugates in targeting Rad23 to the proteasome. Mol. Biol. Cell 18 (2007), 1953–1963.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 1953-1963
    • Ghaboosi, N.1    Deshaies, R.J.2
  • 13
    • 81855184492 scopus 로고    scopus 로고
    • Tail-anchored membrane protein insertion into the endoplasmic reticulum
    • Hegde, R.S., Keenan, R.J., Tail-anchored membrane protein insertion into the endoplasmic reticulum. Nat. Rev. Mol. Cell Biol. 12 (2011), 787–798.
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 787-798
    • Hegde, R.S.1    Keenan, R.J.2
  • 14
    • 79960637590 scopus 로고    scopus 로고
    • Protein targeting and degradation are coupled for elimination of mislocalized proteins
    • Hessa, T., Sharma, A., Mariappan, M., Eshleman, H.D., Gutierrez, E., Hegde, R.S., Protein targeting and degradation are coupled for elimination of mislocalized proteins. Nature 475 (2011), 394–397.
    • (2011) Nature , vol.475 , pp. 394-397
    • Hessa, T.1    Sharma, A.2    Mariappan, M.3    Eshleman, H.D.4    Gutierrez, E.5    Hegde, R.S.6
  • 15
    • 0037144597 scopus 로고    scopus 로고
    • Role of ubiquilin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell death
    • Ko, H.S., Uehara, T., Nomura, Y., Role of ubiquilin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell death. J. Biol. Chem. 277 (2002), 35386–35392.
    • (2002) J. Biol. Chem. , vol.277 , pp. 35386-35392
    • Ko, H.S.1    Uehara, T.2    Nomura, Y.3
  • 16
    • 34250369119 scopus 로고    scopus 로고
    • Protein degradation within mitochondria: versatile activities of AAA proteases and other peptidases
    • Koppen, M., Langer, T., 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
  • 18
    • 84930746830 scopus 로고    scopus 로고
    • The biology of proteostasis in aging and disease
    • Labbadia, J., Morimoto, R.I., The biology of proteostasis in aging and disease. Annu. Rev. Biochem. 84 (2015), 435–464.
    • (2015) Annu. Rev. Biochem. , vol.84 , pp. 435-464
    • Labbadia, J.1    Morimoto, R.I.2
  • 19
    • 84894051837 scopus 로고    scopus 로고
    • Ubiquilin-1 protects cells from oxidative stress and ischemic stroke caused tissue injury in mice
    • Liu, Y., Lü, L., Hettinger, C.L., Dong, G., Zhang, D., Rezvani, K., Wang, X., Wang, H., Ubiquilin-1 protects cells from oxidative stress and ischemic stroke caused tissue injury in mice. J. Neurosci. 34 (2014), 2813–2821.
    • (2014) J. Neurosci. , vol.34 , pp. 2813-2821
    • Liu, Y.1    Lü, L.2    Hettinger, C.L.3    Dong, G.4    Zhang, D.5    Rezvani, K.6    Wang, X.7    Wang, H.8
  • 23
    • 84924362921 scopus 로고    scopus 로고
    • Protein targeting. Structure of the Get3 targeting factor in complex with its membrane protein cargo
    • Mateja, A., Paduch, M., Chang, H.-Y., Szydlowska, A., Kossiakoff, A.A., Hegde, R.S., Keenan, R.J., Protein targeting. Structure of the Get3 targeting factor in complex with its membrane protein cargo. Science 347 (2015), 1152–1155.
    • (2015) Science , vol.347 , pp. 1152-1155
    • Mateja, A.1    Paduch, M.2    Chang, H.-Y.3    Szydlowska, A.4    Kossiakoff, A.A.5    Hegde, R.S.6    Keenan, R.J.7
  • 24
    • 84862765926 scopus 로고    scopus 로고
    • Ubiquilin immunoreactivity in cytoplasmic and nuclear inclusions in synucleinopathies, polyglutamine diseases and intranuclear inclusion body disease
    • Mori, F., Tanji, K., Odagiri, S., Toyoshima, Y., Yoshida, M., Ikeda, T., Sasaki, H., Kakita, A., Takahashi, H., Wakabayashi, K., Ubiquilin immunoreactivity in cytoplasmic and nuclear inclusions in synucleinopathies, polyglutamine diseases and intranuclear inclusion body disease. Acta Neuropathol. 124 (2012), 149–151.
    • (2012) Acta Neuropathol. , vol.124 , pp. 149-151
    • Mori, F.1    Tanji, K.2    Odagiri, S.3    Toyoshima, Y.4    Yoshida, M.5    Ikeda, T.6    Sasaki, H.7    Kakita, A.8    Takahashi, H.9    Wakabayashi, K.10
  • 25
    • 0030969942 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Neupert, W., Protein import into mitochondria. Annu. Rev. Biochem. 66 (1997), 863–917.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 863-917
    • Neupert, W.1
  • 29
    • 84904567733 scopus 로고    scopus 로고
    • Cytosolic quality control of mislocalized proteins requires RNF126 recruitment to Bag6
    • Rodrigo-Brenni, M.C., Gutierrez, E., Hegde, R.S., Cytosolic quality control of mislocalized proteins requires RNF126 recruitment to Bag6. Mol. Cell 55 (2014), 227–237.
    • (2014) Mol. Cell , vol.55 , pp. 227-237
    • Rodrigo-Brenni, M.C.1    Gutierrez, E.2    Hegde, R.S.3
  • 31
    • 84898728074 scopus 로고    scopus 로고
    • Ubiquilin-1 overexpression increases the lifespan and delays accumulation of Huntingtin aggregates in the R6/2 mouse model of Huntington's disease
    • Safren, N., El Ayadi, A., Chang, L., Terrillion, C.E., Gould, T.D., Boehning, D.F., Monteiro, M.J., Ubiquilin-1 overexpression increases the lifespan and delays accumulation of Huntingtin aggregates in the R6/2 mouse model of Huntington's disease. PLoS ONE, 9, 2014, e87513.
    • (2014) PLoS ONE , vol.9 , pp. e87513
    • Safren, N.1    El Ayadi, A.2    Chang, L.3    Terrillion, C.E.4    Gould, T.D.5    Boehning, D.F.6    Monteiro, M.J.7
  • 34
    • 33845685298 scopus 로고    scopus 로고
    • Cytosolic factor- and TOM-independent import of C-tail-anchored mitochondrial outer membrane proteins
    • Setoguchi, K., Otera, H., Mihara, K., Cytosolic factor- and TOM-independent import of C-tail-anchored mitochondrial outer membrane proteins. EMBO J. 25 (2006), 5635–5647.
    • (2006) EMBO J. , vol.25 , pp. 5635-5647
    • Setoguchi, K.1    Otera, H.2    Mihara, K.3
  • 35
    • 84455178968 scopus 로고    scopus 로고
    • A calmodulin-dependent translocation pathway for small secretory proteins
    • Shao, S., Hegde, R.S., A calmodulin-dependent translocation pathway for small secretory proteins. Cell 147 (2011), 1576–1588.
    • (2011) Cell , vol.147 , pp. 1576-1588
    • Shao, S.1    Hegde, R.S.2
  • 36
    • 77954691102 scopus 로고    scopus 로고
    • In vitro dissection of protein translocation into the mammalian endoplasmic reticulum
    • Sharma, A., Mariappan, M., Appathurai, S., Hegde, R.S., In vitro dissection of protein translocation into the mammalian endoplasmic reticulum. Methods Mol. Biol. 619 (2010), 339–363.
    • (2010) Methods Mol. Biol. , vol.619 , pp. 339-363
    • Sharma, A.1    Mariappan, M.2    Appathurai, S.3    Hegde, R.S.4
  • 37
    • 33750008686 scopus 로고    scopus 로고
    • Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements
    • Shiau, A.K., Harris, S.F., Southworth, D.R., Agard, D.A., Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements. Cell 127 (2006), 329–340.
    • (2006) Cell , vol.127 , pp. 329-340
    • Shiau, A.K.1    Harris, S.F.2    Southworth, D.R.3    Agard, D.A.4
  • 40
    • 33947218544 scopus 로고    scopus 로고
    • Identification of a targeting factor for posttranslational membrane protein insertion into the ER
    • Stefanovic, S., Hegde, R.S., Identification of a targeting factor for posttranslational membrane protein insertion into the ER. Cell 128 (2007), 1147–1159.
    • (2007) Cell , vol.128 , pp. 1147-1159
    • Stefanovic, S.1    Hegde, R.S.2
  • 41
    • 68949221689 scopus 로고    scopus 로고
    • Ubiquitin-like and ubiquitin-associated domain proteins: significance in proteasomal degradation
    • Su, V., Lau, A.F., Ubiquitin-like and ubiquitin-associated domain proteins: significance in proteasomal degradation. Cell. Mol. Life Sci. 66 (2009), 2819–2833.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 2819-2833
    • Su, V.1    Lau, A.F.2
  • 42
    • 84971516837 scopus 로고    scopus 로고
    • UBQLN4 recognizes mislocalized transmembrane domain proteins and targets these to proteasomal degradation
    • Published online April 22, 2016
    • Suzuki, R., Kawahara, H., UBQLN4 recognizes mislocalized transmembrane domain proteins and targets these to proteasomal degradation. EMBO Rep., 2016, 10.15252/embr.201541402 Published online April 22, 2016.
    • (2016) EMBO Rep.
    • Suzuki, R.1    Kawahara, H.2
  • 43
    • 84940517301 scopus 로고    scopus 로고
    • A cytosolic network suppressing mitochondria-mediated proteostatic stress and cell death
    • Wang, X., Chen, X.J., A cytosolic network suppressing mitochondria-mediated proteostatic stress and cell death. Nature 524 (2015), 481–484.
    • (2015) Nature , vol.524 , pp. 481-484
    • Wang, X.1    Chen, X.J.2
  • 44
    • 34447095637 scopus 로고    scopus 로고
    • Ubiquilin interacts and enhances the degradation of expanded-polyglutamine proteins
    • Wang, H., Monteiro, M.J., Ubiquilin interacts and enhances the degradation of expanded-polyglutamine proteins. Biochem. Biophys. Res. Commun. 360 (2007), 423–427.
    • (2007) Biochem. Biophys. Res. Commun. , vol.360 , pp. 423-427
    • Wang, H.1    Monteiro, M.J.2
  • 45
    • 77957376226 scopus 로고    scopus 로고
    • A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum
    • Wang, F., Brown, E.C., Mak, G., Zhuang, J., Denic, V., A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum. Mol. Cell 40 (2010), 159–171.
    • (2010) Mol. Cell , vol.40 , pp. 159-171
    • Wang, F.1    Brown, E.C.2    Mak, G.3    Zhuang, J.4    Denic, V.5
  • 46
    • 84897129156 scopus 로고    scopus 로고
    • Differential scales of protein quality control
    • Wolff, S., Weissman, J.S., Dillin, A., Differential scales of protein quality control. Cell 157 (2014), 52–64.
    • (2014) Cell , vol.157 , pp. 52-64
    • Wolff, S.1    Weissman, J.S.2    Dillin, A.3
  • 47
    • 0035242370 scopus 로고    scopus 로고
    • Oxidative stress inhibits the mitochondrial import of preproteins and leads to their degradation
    • Wright, G., Terada, K., Yano, M., Sergeev, I., Mori, M., Oxidative stress inhibits the mitochondrial import of preproteins and leads to their degradation. Exp. Cell Res. 263 (2001), 107–117.
    • (2001) Exp. Cell Res. , vol.263 , pp. 107-117
    • Wright, G.1    Terada, K.2    Yano, M.3    Sergeev, I.4    Mori, M.5
  • 49
    • 0037428164 scopus 로고    scopus 로고
    • Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70
    • Young, J.C., Hoogenraad, N.J., Hartl, F.U., Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70. Cell 112 (2003), 41–50.
    • (2003) Cell , vol.112 , pp. 41-50
    • Young, J.C.1    Hoogenraad, N.J.2    Hartl, F.U.3
  • 50
    • 39649120317 scopus 로고    scopus 로고
    • Affinity makes the difference: nonselective interaction of the UBA domain of ubiquilin-1 with monomeric ubiquitin and polyubiquitin chains
    • Zhang, D., Raasi, S., Fushman, D., Affinity makes the difference: nonselective interaction of the UBA domain of ubiquilin-1 with monomeric ubiquitin and polyubiquitin chains. J. Mol. Biol. 377 (2008), 162–180.
    • (2008) J. Mol. Biol. , vol.377 , pp. 162-180
    • Zhang, D.1    Raasi, S.2    Fushman, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.