메뉴 건너뛰기




Volumn 475, Issue 7356, 2011, Pages 394-399

Protein targeting and degradation are coupled for elimination of mislocalized proteins

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; CHAPERONE PROTEIN BAG6; MEMBRANE PROTEIN; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 79960637590     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature10181     Document Type: Article
Times cited : (220)

References (38)
  • 2
    • 10644267669 scopus 로고    scopus 로고
    • Protection from cytosolic prion protein toxicity by modulation of protein translocation
    • DOI 10.1038/sj.emboj.7600462
    • Rane, N. S., Yonkovich, J. L. & Hegde, R. S. Protection from cytosolic prion protein toxicity by modulation of protein translocation. EMBO J. 23, 4550-4559 (2004). (Pubitemid 39657855)
    • (2004) EMBO Journal , vol.23 , Issue.23 , pp. 4550-4559
    • Rane, N.S.1    Yonkovich, J.L.2    Hegde, R.S.3
  • 3
    • 33751333201 scopus 로고    scopus 로고
    • Substrate-specific translocational attenuation during ER stress defines a pre-emptive quality control pathway
    • Kang, S. W. et al. Substrate-specific translocational attenuation during ER stress defines a pre-emptive quality control pathway. Cell 127, 999-1013 (2006).
    • (2006) Cell , vol.127 , pp. 999-1013
    • Kang, S.W.1
  • 4
    • 77956183398 scopus 로고    scopus 로고
    • A ribosome-associating factor chaperones tail-anchored membrane proteins
    • Mariappan, M. et al. A ribosome-associating factor chaperones tail-anchored membrane proteins. Nature 466, 1120-1124 (2010).
    • (2010) Nature , vol.466 , pp. 1120-1124
    • Mariappan, M.1
  • 5
    • 0036481454 scopus 로고    scopus 로고
    • Signal sequences control gating of the protein translocation channel in a substrate-specific manner
    • DOI 10.1016/S1534-5807(01)00120-4, PII S1534580701001204
    • Kim, S. J., Mitra, D., Salerno, J. R. & Hegde, R. S. Signal sequences control gating of the protein translocation channel in a substrate-specific manner. Dev. Cell 2, 207-217 (2002). (Pubitemid 38351585)
    • (2002) Developmental Cell , vol.2 , Issue.2 , pp. 207-217
    • Kim, S.J.1    Mitra, D.2    Salerno, J.R.3    Hegde, R.S.4
  • 6
    • 11144255136 scopus 로고    scopus 로고
    • The efficiency of protein compartmentalization into the secretory pathway
    • DOI 10.1091/mbc.E04-06-0508
    • Levine, C. G., Mitra, D., Sharma, A., Smith, C. L. & Hegde, R. S. The efficiency of protein compartmentalization into the secretory pathway. Mol. Biol. Cell 16, 279-291 (2005). (Pubitemid 40024310)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.1 , pp. 279-291
    • Levine, C.G.1    Mitra, D.2    Sharma, A.3    Smith, C.L.4    Hegde, R.S.5
  • 7
    • 0036854303 scopus 로고    scopus 로고
    • Cotranslational partitioning of nascent prion protein into multiple populations at the translocation channel
    • DOI 10.1091/mbc.E02-05-0293
    • Kim, S. J. & Hegde, R. S. Cotranslational partitioning of nascent prion protein into multiple populations at the translocation channel. Mol. Biol. Cell 13, 3775-3786 (2002). (Pubitemid 35398547)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.11 , pp. 3775-3786
    • Kim, S.J.1    Hegde, R.S.2
  • 8
    • 77149179440 scopus 로고    scopus 로고
    • Signal sequence insufficiency contributes to neurodegeneration caused by transmembrane prion protein
    • Rane, N. S., Chakrabarti, O., Feigenbaum, L. & Hegde, R. S. Signal sequence insufficiency contributes to neurodegeneration caused by transmembrane prion protein. J. Cell Biol. 188, 515-526 (2010).
    • (2010) J. Cell Biol. , vol.188 , Issue.515-526
    • Rane, N.S.1    Chakrabarti, O.2    Feigenbaum, L.3    Hegde, R.S.4
  • 9
    • 33750087269 scopus 로고    scopus 로고
    • Conditions of endoplasmic reticulum stress favor the accumulation of cytosolic prion protein
    • DOI 10.1074/jbc.M605320200
    • Orsi, A., Fioriti, L., Chiesa, R. & Sitia, R. Conditions of endoplasmic reticulumstress favor the accumulation of cytosolic prion protein. J. Biol. Chem. 281, 30431-30438 (2006). (Pubitemid 44582099)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.41 , pp. 30431-30438
    • Orsi, A.1    Fioriti, L.2    Chiesa, R.3    Sitia, R.4
  • 11
    • 0037195617 scopus 로고    scopus 로고
    • Sc-like conformation in the cytosol
    • DOI 10.1126/science.1073619
    • Ma, J. & Lindquist, S. Conversion of PrP to a self-perpetuating PrPSc-like conformation in the cytosol. Science 298, 1785-1788 (2002). (Pubitemid 35404121)
    • (2002) Science , vol.298 , Issue.5599 , pp. 1785-1788
    • Ma, J.1    Lindquist, S.2
  • 12
    • 66449124518 scopus 로고    scopus 로고
    • Functional depletion of mahogunin by cytosolically exposed prion protein contributes to neurodegeneration
    • Chakrabarti, O. & Hegde, R. S. Functional depletion of mahogunin by cytosolically exposed prion protein contributes to neurodegeneration. Cell 137, 1136-1147 (2009).
    • (2009) Cell , vol.137 , pp. 1136-1147
    • Chakrabarti, O.1    Hegde, R.S.2
  • 13
    • 0037195647 scopus 로고    scopus 로고
    • Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol
    • DOI 10.1126/science.1073725
    • Ma, J., Wollmann, R. & Lindquist, S. Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol. Science 298, 1781-1785 (2002). (Pubitemid 35404120)
    • (2002) Science , vol.298 , Issue.5599 , pp. 1781-1785
    • Ma, J.1    Wollmann, R.2    Lindquist, S.3
  • 14
    • 51449098355 scopus 로고    scopus 로고
    • Reduced translocation of nascent prion protein during ER stress contributes to neurodegeneration
    • Rane, N. S., Kang, S. W., Chakrabarti, O., Feigenbaum, L. & Hegde, R. S. Reduced translocation of nascent prion protein during ER stress contributes to neurodegeneration. Dev. Cell 15, 359-370 (2008).
    • (2008) Dev. Cell , vol.15 , pp. 359-370
    • Rane, N.S.1    Kang, S.W.2    Chakrabarti, O.3    Feigenbaum, L.4    Hegde, R.S.5
  • 15
    • 78649357985 scopus 로고    scopus 로고
    • Protein quality control in the cytosol and the endoplasmic reticulum: Brothers in arms
    • Buchberger, A., Bukau, B. & Sommer, T. Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms. Mol. Cell 40, 238-252 (2010).
    • (2010) Mol. Cell , vol.40 , pp. 238-252
    • Buchberger, A.1    Bukau, B.2    Sommer, T.3
  • 16
    • 1242291789 scopus 로고    scopus 로고
    • CHIP: A link between the chaperone and proteasome systems
    • DOI 10.1379/1466-1268(2003)008<0303:CALBTC>2.0.CO;2
    • McDonough, H. & Patterson, C. CHIP: a link between the chaperone and proteasome systems. Cell Stress Chaperones 8, 303-308 (2003). (Pubitemid 38222876)
    • (2003) Cell Stress and Chaperones , vol.8 , Issue.4 , pp. 303-308
    • McDonough, H.1    Patterson, C.2
  • 17
    • 77954352789 scopus 로고    scopus 로고
    • Bat3 promotes the membrane integration of tail-anchored proteins
    • Leznicki, P., Clancy, A., Schwappach, B. & High, S. Bat3 promotes the membrane integration of tail-anchored proteins. J. Cell Sci. 123, 2170-2178 (2010).
    • (2010) J. Cell Sci. , vol.123 , pp. 2170-2178
    • Leznicki, P.1    Clancy, A.2    Schwappach, B.3    High, S.4
  • 18
    • 60849096653 scopus 로고    scopus 로고
    • A signal-anchor sequence stimulates signal recognition particle binding to ribosomes from inside the exit tunnel
    • Berndt, U., Oellerer, S., Zhang, Y., Johnson, A. E. & Rospert, S. A signal-anchor sequence stimulates signal recognition particle binding to ribosomes from inside the exit tunnel. Proc. Natl Acad. Sci. USA 106, 1398-1403 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 1398-1403
    • Berndt, U.1    Oellerer, S.2    Zhang, Y.3    Johnson, A.E.4    Rospert, S.5
  • 20
    • 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, 1147-1159 (2007).
    • (2007) Cell , vol.128 , pp. 1147-1159
    • Stefanovic, S.1    Hegde, R.S.2
  • 21
    • 0344688165 scopus 로고    scopus 로고
    • Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region
    • DOI 10.1016/S0888-7543(03)00235-0
    • Lehner, B. et al. Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region. Genomics 83, 153-167 (2004). (Pubitemid 37518270)
    • (2004) Genomics , vol.83 , Issue.1 , pp. 153-167
    • Lehner, B.1    Semple, J.I.2    Brown, S.E.3    Counsell, D.4    Campbell, R.D.5    Sanderson, C.M.6
  • 22
    • 33846107847 scopus 로고    scopus 로고
    • The cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome system
    • Park, S. H. et al. The cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome system. Mol. Biol. Cell 18, 153-165 (2007).
    • (2007) Mol. Biol. Cell , vol.18 , pp. 153-165
    • Park, S.H.1
  • 23
    • 57049182407 scopus 로고    scopus 로고
    • Degradation of misfolded protein in the cytoplasm is mediated by the ubiquitin ligase Ubr1
    • Eisele, F. & Wolf, D. H. Degradation of misfolded protein in the cytoplasm is mediated by the ubiquitin ligase Ubr1. FEBS Lett. 582, 4143-4146 (2008).
    • (2008) FEBS Lett. , vol.582 , pp. 4143-4146
    • Eisele, F.1    Wolf, D.H.2
  • 24
    • 75749101057 scopus 로고    scopus 로고
    • Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1
    • Heck, J. W., Cheung, S. K. & Hampton, R. Y. Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1. Proc. Natl Acad. Sci. USA 107, 1106-1111 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 1106-1111
    • Heck, J.W.1    Cheung, S.K.2    Hampton, R.Y.3
  • 25
    • 77954196466 scopus 로고    scopus 로고
    • Ubr1 and Ubr2 function in a quality control pathway for degradation of unfolded cytosolic proteins
    • Nillegoda, N. B. et al. Ubr1 and Ubr2 function in a quality control pathway for degradation of unfolded cytosolic proteins. Mol. Biol. Cell 21, 2102-2116 (2010).
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2102-2116
    • Nillegoda, N.B.1
  • 26
    • 77955878748 scopus 로고    scopus 로고
    • BAG-6 is essential for selective elimination of defective proteasomal substrates
    • Minami, R. et al. BAG-6 is essential for selective elimination of defective proteasomal substrates. J. Cell Biol. 190, 637-650 (2010).
    • (2010) J. Cell Biol. , vol.190 , pp. 637-650
    • Minami, R.1
  • 27
    • 79953687692 scopus 로고    scopus 로고
    • Enzymatic blockade of the ubiquitin-proteasome pathway
    • Ernst, R. et al. Enzymatic blockade of the ubiquitin-proteasome pathway. PLoS Biol. 8, e1000605 (2011).
    • (2011) PLoS Biol , vol.8
    • Ernst, R.1
  • 28
    • 79959347089 scopus 로고    scopus 로고
    • A chaperone holdasemaintains polypeptides in soluble states for proteasomedegradation
    • doi:10.1016/j.molcel.2011.05.010(in thepress
    • Wang, Q. et al. A chaperone holdasemaintains polypeptides in soluble states for proteasomedegradation. Mol.Cell doi:10.1016/j.molcel.2011.05.010(in thepress).
    • Mol.Cell
    • Wang, Q.1
  • 29
    • 22444450987 scopus 로고    scopus 로고
    • A substrate-specific inhibitor of protein translocation into the endoplasmic reticulum
    • DOI 10.1038/nature03821
    • Garrison, J. L., Kunkel, E. J., Hegde, R. S. & Taunton, J. A substrate-specific inhibitor of protein translocation into the endoplasmic reticulum. Nature 436, 285-289 (2005). (Pubitemid 41021282)
    • (2005) Nature , vol.436 , Issue.7048 , pp. 285-289
    • Garrison, J.L.1    Kunkel, E.J.2    Hegde, R.S.3    Taunton, J.4
  • 30
    • 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, 339-363 (2010).
    • (2010) Methods Mol. Biol. , vol.619 , pp. 339-363
    • Sharma, A.1    Mariappan, M.2    Appathurai, S.3    Hegde, R.S.4
  • 31
    • 78650434660 scopus 로고    scopus 로고
    • Compartmentrestricted biotinylation reveals novel features of prion protein metabolism in vivo
    • Emerman, A. B., Zhang, Z. R., Chakrabarti, O. & Hegde, R. S. Compartmentrestricted biotinylation reveals novel features of prion protein metabolism in vivo. Mol. Biol. Cell 21, 4325-4337 (2010).
    • (2010) Mol. Biol. Cell , vol.21 , pp. 4325-4337
    • Emerman, A.B.1    Zhang, Z.R.2    Chakrabarti, O.3    Hegde, R.S.4
  • 32
    • 54249087710 scopus 로고    scopus 로고
    • Retrotranslocation of prion proteins fromthe endoplasmic reticulumby preventing GPI signal transamidation
    • Ashok, A.&Hegde, R. S. Retrotranslocation of prion proteins fromthe endoplasmic reticulumby preventing GPI signal transamidation. Mol. Biol. Cell 19, 3463-3476 (2008).
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3463-3476
    • Ashok, A.1    Hegde, R.S.2
  • 35
    • 77954047969 scopus 로고    scopus 로고
    • MultilayeredmechanismofCD4 downregulation by HIV-1Vpu involving distinct ER retention and ERAD targeting steps
    • Magadán, J. G. et al.MultilayeredmechanismofCD4 downregulation by HIV-1Vpu involving distinct ER retention and ERAD targeting steps. PLoS Pathogens 6, e1000869 (2010).
    • (2010) PLoS Pathogens , vol.6
    • Magadán, J.G.1
  • 36
    • 0037450802 scopus 로고    scopus 로고
    • Substrate-specific function of the translocon-associated protein complex during translocation across the ER membrane
    • DOI 10.1083/jcb.200210095
    • 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, 529-539 (2003). (Pubitemid 36254391)
    • (2003) Journal of Cell Biology , vol.160 , Issue.4 , pp. 529-539
    • Fons, R.D.1    Bogert, B.A.2    Hegde, R.S.3
  • 37
    • 0020357598 scopus 로고
    • Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle
    • DOI 10.1083/jcb.95.2.463
    • Gilmore, R., Blobel, G. & Walter, P. Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle. J. Cell Biol. 95, 463-469 (1982). (Pubitemid 13215861)
    • (1982) Journal of Cell Biology , vol.95 , Issue.2 I , pp. 463-469
    • Gilmore, R.1    Blobel, G.2    Walter, P.3
  • 38
    • 0005614190 scopus 로고
    • Photocrosslinking of the signal sequence of nascent preprolactin to the 54-kilodalton polypeptide of the signal recognition particle
    • DOI 10.1073/pnas.83.22.8604
    • Krieg, U. C., Walter, P. & Johnson, A. E. Photocrosslinking of the signal sequence of nascent preprolactin to the 54-kilodalton polypeptide of the signal recognition particle. Proc. Natl Acad. Sci. USA 83, 8604-8608 (1986). (Pubitemid 17194918)
    • (1986) Proceedings of the National Academy of Sciences of the United States of America , vol.83 , Issue.22 , pp. 8604-8608
    • Krieg, U.C.1    Walter, P.2    Johnson, A.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.