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Volumn 209, Issue 2, 2015, Pages 261-273

The yeast ERAD-C ubiquitin ligase Doa10 recognizes an intramembrane degron

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; SERINE; TRANSMEMBRANE PROTEIN SEC61 BETA SUBUNIT HOMOLOGUE 2; UBIQUITIN PROTEIN LIGASE; UBIQUITIN PROTEIN LIGASE DOA10; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; CARRIER PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; SBH2 PROTEIN, S CEREVISIAE; SSM4 PROTEIN, S CEREVISIAE; UBIQUITIN;

EID: 84980051722     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201408088     Document Type: Article
Times cited : (63)

References (59)
  • 1
    • 84904312891 scopus 로고    scopus 로고
    • A cytosolic degradation pathway, prERAD, monitors pre-inserted secretory pathway proteins
    • Ast, T., N. Aviram, S.G. Chuartzman, and M. Schuldiner. 2014. A cytosolic degradation pathway, prERAD, monitors pre-inserted secretory pathway proteins. J. Cell Sci. 127:3017-3023. http://dx.doi.org/10.1242/jcs.144386
    • (2014) J. Cell Sci , vol.127 , pp. 3017-3023
    • Ast, T.1    Aviram, N.2    Chuartzman, S.G.3    Schuldiner, M.4
  • 2
    • 0346373729 scopus 로고    scopus 로고
    • Downregulation of major histocompatibility complex class I by human ubiquitin ligases related to viral immune evasion proteins
    • Bartee, E., M. Mansouri, B.T. Hovey Nerenberg, K. Gouveia, and K. Früh. 2004. Downregulation of major histocompatibility complex class I by human ubiquitin ligases related to viral immune evasion proteins. J. Virol. 78:1109-1120. http://dx.doi.org/10.1128/JVI.78.3.1109-1120.2004
    • (2004) J. Virol , vol.78 , pp. 1109-1120
    • Bartee, E.1    Mansouri, M.2    Hovey Nerenberg, B.T.3    Gouveia, K.4    Früh, K.5
  • 3
    • 0035144199 scopus 로고    scopus 로고
    • Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation
    • Bays, N.W., R.G. Gardner, L.P. Seelig, C.A. Joazeiro, and R.Y. Hampton. 2001. Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation. Nat. Cell Biol. 3:24-29. http://dx.doi.org/10.1038/35050524
    • (2001) Nat. Cell Biol , vol.3 , pp. 24-29
    • Bays, N.W.1    Gardner, R.G.2    Seelig, L.P.3    Joazeiro, C.A.4    Hampton, R.Y.5
  • 5
    • 0029985369 scopus 로고    scopus 로고
    • Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway
    • Biederer, T., C. Volkwein, and T. Sommer. 1996. Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway. EMBO J. 15:2069-2076.
    • (1996) EMBO J , vol.15 , pp. 2069-2076
    • Biederer, T.1    Volkwein, C.2    Sommer, T.3
  • 6
    • 0024345717 scopus 로고
    • Pre-Golgi degradation of newly synthesized T-cell antigen receptor chains: intrinsic sensitivity and the role of subunit assembly
    • Bonifacino, J.S., C.K. Suzuki, J. Lippincott-Schwartz, A.M. Weissman, and R.D. Klausner. 1989. Pre-Golgi degradation of newly synthesized T-cell antigen receptor chains: intrinsic sensitivity and the role of subunit assembly. J. Cell Biol. 109:73-83. http://dx.doi.org/10.1083/jcb.109.1.73
    • (1989) J. Cell Biol , vol.109 , pp. 73-83
    • Bonifacino, J.S.1    Suzuki, C.K.2    Lippincott-Schwartz, J.3    Weissman, A.M.4    Klausner, R.D.5
  • 7
    • 0025012782 scopus 로고
    • A peptide sequence confers retention and rapid degradation in the endoplasmic reticulum
    • Bonifacino, J.S., C.K. Suzuki, and R.D. Klausner. 1990. A peptide sequence confers retention and rapid degradation in the endoplasmic reticulum. Science. 247:79-82. http://dx.doi.org/10.1126/science.2294595
    • (1990) Science , vol.247 , pp. 79-82
    • Bonifacino, J.S.1    Suzuki, C.K.2    Klausner, R.D.3
  • 8
    • 79960711299 scopus 로고    scopus 로고
    • Protein folding and quality control in the endoplasmic reticulum: Recent lessons from yeast and mammalian cell systems
    • Brodsky, J.L., and W.R. Skach. 2011. Protein folding and quality control in the endoplasmic reticulum: Recent lessons from yeast and mammalian cell systems. Curr. Opin. Cell Biol. 23:464-475. http://dx.doi.org/10.1016/j.ceb.2011.05.004
    • (2011) Curr. Opin. Cell Biol , vol.23 , pp. 464-475
    • Brodsky, J.L.1    Skach, W.R.2
  • 9
    • 33746228127 scopus 로고    scopus 로고
    • Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins
    • Carvalho, P., V. Goder, and T.A. Rapoport. 2006. Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins. Cell. 126:361-373. http://dx.doi.org/10.1016/j.cell.2006.05.043
    • (2006) Cell , vol.126 , pp. 361-373
    • Carvalho, P.1    Goder, V.2    Rapoport, T.A.3
  • 10
    • 84898729879 scopus 로고    scopus 로고
    • Cleaning up in the endoplasmic reticulum: ubiquitin in charge
    • Christianson, J.C., and Y. Ye. 2014. Cleaning up in the endoplasmic reticulum: ubiquitin in charge. Nat. Struct. Mol. Biol. 21:325-335. http://dx.doi.org/10.1038/nsmb.2793
    • (2014) Nat. Struct. Mol. Biol , vol.21 , pp. 325-335
    • Christianson, J.C.1    Ye, Y.2
  • 11
    • 80054829298 scopus 로고    scopus 로고
    • Ubiquitin-mediated regulation of CD86 protein expression by the ubiquitin ligase membrane-associated RING-CH-1 (MARCH1)
    • Corcoran, K., M. Jabbour, C. Bhagwandin, M.J. Deymier, D.L. Theisen, and L. Lybarger. 2011. Ubiquitin-mediated regulation of CD86 protein expression by the ubiquitin ligase membrane-associated RING-CH-1 (MARCH1). J. Biol. Chem. 286:37168-37180. http://dx.doi.org/10.1074/jbc.M110.204040
    • (2011) J. Biol. Chem , vol.286 , pp. 37168-37180
    • Corcoran, K.1    Jabbour, M.2    Bhagwandin, C.3    Deymier, M.J.4    Theisen, D.L.5    Lybarger, L.6
  • 12
    • 0034971266 scopus 로고    scopus 로고
    • A viral protein that selectively downregulates ICAM-1 and B7-2 and modulates T cell costimulation
    • Coscoy, L., and D. Ganem. 2001. A viral protein that selectively downregulates ICAM-1 and B7-2 and modulates T cell costimulation. J. Clin. Invest. 107:1599-1606. http://dx.doi.org/10.1172/JCI12432
    • (2001) J. Clin. Invest , vol.107 , pp. 1599-1606
    • Coscoy, L.1    Ganem, D.2
  • 13
    • 0035815754 scopus 로고    scopus 로고
    • Membrane topology and function of Der3/Hrd1p as a ubiquitin-protein ligase (E3) involved in endoplasmic reticulum degradation
    • Deak, P.M., and D.H. Wolf. 2001. Membrane topology and function of Der3/Hrd1p as a ubiquitin-protein ligase (E3) involved in endoplasmic reticulum degradation. J. Biol. Chem. 276:10663-10669. http://dx.doi.org/10.1074/jbc.M008608200
    • (2001) J. Biol. Chem , vol.276 , pp. 10663-10669
    • Deak, P.M.1    Wolf, D.H.2
  • 14
    • 33750349837 scopus 로고    scopus 로고
    • Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase
    • Deng, M., and M. Hochstrasser. 2006. Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase. Nature. 443:827-831. http://dx.doi.org/10.1038/nature05170
    • (2006) Nature , vol.443 , pp. 827-831
    • Deng, M.1    Hochstrasser, M.2
  • 15
    • 84881536447 scopus 로고    scopus 로고
    • Quality control of integral membrane proteins by assembly-dependent membrane integration
    • Feige, M.J., and L.M. Hendershot. 2013. Quality control of integral membrane proteins by assembly-dependent membrane integration. Mol. Cell. 51:297-309. http://dx.doi.org/10.1016/j.molcel.2013.07.013
    • (2013) Mol. Cell , vol.51 , pp. 297-309
    • Feige, M.J.1    Hendershot, L.M.2
  • 16
    • 35649013761 scopus 로고    scopus 로고
    • The transmembrane domain is sufficient for Sbh1p function, its association with the Sec61 complex, and interaction with Rtn1p
    • Feng, D., X. Zhao, C. Soromani, J. Toikkanen, K. Römisch, S.S. Vembar, J.L. Brodsky, S. Keränen, and J. Jäntti. 2007. The transmembrane domain is sufficient for Sbh1p function, its association with the Sec61 complex, and interaction with Rtn1p. J. Biol. Chem. 282:30618-30628. http://dx.doi.org/10.1074/jbc.M701840200
    • (2007) J. Biol. Chem , vol.282 , pp. 30618-30628
    • Feng, D.1    Zhao, X.2    Soromani, C.3    Toikkanen, J.4    Römisch, K.5    Vembar, S.S.6    Brodsky, J.L.7    Keränen, S.8    Jäntti, J.9
  • 17
    • 0029881380 scopus 로고    scopus 로고
    • A second trimeric complex containing homologs of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiae
    • Finke, K., K. Plath, S. Panzner, S. Prehn, T.A. Rapoport, E. Hartmann, and T. Sommer. 1996. A second trimeric complex containing homologs of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiae. EMBO J. 15:1482-1494.
    • (1996) EMBO J , vol.15 , pp. 1482-1494
    • Finke, K.1    Plath, K.2    Panzner, S.3    Prehn, S.4    Rapoport, T.A.5    Hartmann, E.6    Sommer, T.7
  • 18
    • 84867176120 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system of Saccharomyces cerevisiae
    • Finley, D., H.D. Ulrich, T. Sommer, and P. Kaiser. 2012. The ubiquitin-proteasome system of Saccharomyces cerevisiae. Genetics. 192:319-360. http://dx.doi.org/10.1534/genetics.112.140467
    • (2012) Genetics , vol.192 , pp. 319-360
    • Finley, D.1    Ulrich, H.D.2    Sommer, T.3    Kaiser, P.4
  • 19
    • 84880707873 scopus 로고    scopus 로고
    • Sterol homeostasis requires regulated degradation of squalene monooxygenase by the ubiquitin ligase Doa10/Teb4
    • Foresti, O., A. Ruggiano, H.K. Hannibal-Bach, C.S. Ejsing, and P. Carvalho. 2013. Sterol homeostasis requires regulated degradation of squalene monooxygenase by the ubiquitin ligase Doa10/Teb4. eLife. 2:e00953. http://dx.doi.org/10.7554/eLife.00953
    • (2013) eLife , vol.2
    • Foresti, O.1    Ruggiano, A.2    Hannibal-Bach, H.K.3    Ejsing, C.S.4    Carvalho, P.5
  • 20
    • 0033231014 scopus 로고    scopus 로고
    • A 'distributed degron' allows regulated entry into the ER degradation pathway
    • Gardner, R.G., and R.Y. Hampton. 1999. A 'distributed degron' allows regulated entry into the ER degradation pathway. EMBO J. 18:5994-6004. http://dx.doi.org/10.1093/emboj/18.21.5994
    • (1999) EMBO J , vol.18 , pp. 5994-6004
    • Gardner, R.G.1    Hampton, R.Y.2
  • 21
    • 0025994140 scopus 로고
    • Guide to yeast genetics and molecular biology
    • Academic Press, San Diego
    • Guthrie, C., and G. Fink, editors. 1991. Guide to yeast genetics and molecular biology. Methods in Enzymology. Vol. 194. Academic Press, San Diego.
    • (1991) Methods in Enzymology , vol.194
    • Guthrie, C.1    Fink, G.2
  • 22
    • 81855184492 scopus 로고    scopus 로고
    • Tail-anchored membrane protein insertion into the endoplasmic reticulum
    • Hegde, R.S., and R.J. Keenan. 2011. Tail-anchored membrane protein insertion into the endoplasmic reticulum. Nat. Rev. Mol. Cell Biol. 12:787-798. http://dx.doi.org/10.1038/nrm3226
    • (2011) Nat. Rev. Mol. Cell Biol , vol.12 , pp. 787-798
    • Hegde, R.S.1    Keenan, R.J.2
  • 23
    • 77955049339 scopus 로고    scopus 로고
    • Quality and quantity control at the endoplasmic reticulum
    • Hegde, R.S., and H.L. Ploegh. 2010. Quality and quantity control at the endoplasmic reticulum. Curr. Opin. Cell Biol. 22:437-446. http://dx.doi.org/10.1016/j.ceb.2010.05.005
    • (2010) Curr. Opin. Cell Biol , vol.22 , pp. 437-446
    • Hegde, R.S.1    Ploegh, H.L.2
  • 24
    • 0034651604 scopus 로고    scopus 로고
    • Degradation of unassembled Vph1p reveals novel aspects of the yeast ER quality control system
    • Hill, K., and A.A. Cooper. 2000. Degradation of unassembled Vph1p reveals novel aspects of the yeast ER quality control system. EMBO J. 19:550-561. http://dx.doi.org/10.1093/emboj/19.4.550
    • (2000) EMBO J , vol.19 , pp. 550-561
    • Hill, K.1    Cooper, A.A.2
  • 25
    • 63649161943 scopus 로고    scopus 로고
    • The ubiquitylation machinery of the endoplasmic reticulum
    • Hirsch, C., R. Gauss, S.C. Horn, O. Neuber, and T. Sommer. 2009. The ubiquitylation machinery of the endoplasmic reticulum. Nature. 458:453-460. http://dx.doi.org/10.1038/nature07962
    • (2009) Nature , vol.458 , pp. 453-460
    • Hirsch, C.1    Gauss, R.2    Horn, S.C.3    Neuber, O.4    Sommer, T.5
  • 26
    • 63649113699 scopus 로고    scopus 로고
    • Origin and function of ubiquitin-like proteins
    • Hochstrasser, M. 2009. Origin and function of ubiquitin-like proteins. Nature. 458:422-429. http://dx.doi.org/10.1038/nature07958
    • (2009) Nature , vol.458 , pp. 422-429
    • Hochstrasser, M.1
  • 27
    • 4444355303 scopus 로고    scopus 로고
    • Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble luminal protein
    • Huyer, G., W.F. Piluek, Z. Fansler, S.G. Kreft, M. Hochstrasser, J.L. Brodsky, and S. Michaelis. 2004. Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble luminal protein. J. Biol. Chem. 279:38369-38378. http://dx.doi.org/10.1074/jbc.M402468200
    • (2004) J. Biol. Chem , vol.279 , pp. 38369-38378
    • Huyer, G.1    Piluek, W.F.2    Fansler, Z.3    Kreft, S.G.4    Hochstrasser, M.5    Brodsky, J.L.6    Michaelis, S.7
  • 28
    • 0036525752 scopus 로고    scopus 로고
    • Sec61β-a component of the archaeal protein secretory system
    • Kinch, L.N., M.H. Saier Jr., and N.V. Grishin. 2002. Sec61β-a component of the archaeal protein secretory system. Trends Biochem. Sci. 27:170-171. http://dx.doi.org/10.1016/S0968-0004(01)02055-2
    • (2002) Trends Biochem. Sci , vol.27 , pp. 170-171
    • Kinch, L.N.1    Saier, M.H.2    Grishin, N.V.3
  • 29
    • 79958015229 scopus 로고    scopus 로고
    • An unusual transmembrane helix in the endoplasmic reticulum ubiquitin ligase Doa10 modulates degradation of its cognate E2 enzyme
    • Kreft, S.G., and M. Hochstrasser. 2011. An unusual transmembrane helix in the endoplasmic reticulum ubiquitin ligase Doa10 modulates degradation of its cognate E2 enzyme. J. Biol. Chem. 286:20163-20174. http://dx.doi.org/10.1074/jbc.M110.196360
    • (2011) J. Biol. Chem , vol.286 , pp. 20163-20174
    • Kreft, S.G.1    Hochstrasser, M.2
  • 30
    • 33646185061 scopus 로고    scopus 로고
    • Membrane topology of the yeast endoplasmic reticulum-localized ubiquitin ligase Doa10 and comparison with its human ortholog TEB4 (MARCH-VI)
    • Kreft, S.G., L. Wang, and M. Hochstrasser. 2006. Membrane topology of the yeast endoplasmic reticulum-localized ubiquitin ligase Doa10 and comparison with its human ortholog TEB4 (MARCH-VI). J. Biol. Chem. 281:4646-4653. http://dx.doi.org/10.1074/jbc.M512215200
    • (2006) J. Biol. Chem , vol.281 , pp. 4646-4653
    • Kreft, S.G.1    Wang, L.2    Hochstrasser, M.3
  • 31
    • 0032189348 scopus 로고    scopus 로고
    • Proteasome inhibitors: valuable new tools for cell biologists
    • Lee, D.H., and A.L. Goldberg. 1998. Proteasome inhibitors: valuable new tools for cell biologists. Trends Cell Biol. 8:397-403. http://dx.doi.org/10.1016/S0962-8924(98)01346-4
    • (1998) Trends Cell Biol , vol.8 , pp. 397-403
    • Lee, D.H.1    Goldberg, A.L.2
  • 32
    • 57549089212 scopus 로고    scopus 로고
    • Inter-species complementation of the translocon beta subunit requires only its transmembrane domain
    • Leroux, A., and L.A. Rokeach. 2008. Inter-species complementation of the translocon beta subunit requires only its transmembrane domain. PLoS ONE. 3:e3880. http://dx.doi.org/10.1371/journal.pone.0003880
    • (2008) PLoS ONE , vol.3
    • Leroux, A.1    Rokeach, L.A.2
  • 33
    • 0031690373 scopus 로고    scopus 로고
    • Ste6p mutants defective in exit from the endoplasmic reticulum (ER) reveal aspects of an ER quality control pathway in Saccharomyces cerevisiae
    • Loayza, D., A. Tam, W.K. Schmidt, and S. Michaelis. 1998. Ste6p mutants defective in exit from the endoplasmic reticulum (ER) reveal aspects of an ER quality control pathway in Saccharomyces cerevisiae. Mol. Biol. Cell. 9:2767-2784. http://dx.doi.org/10.1091/mbc.9.10.2767
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2767-2784
    • Loayza, D.1    Tam, A.2    Schmidt, W.K.3    Michaelis, S.4
  • 34
    • 84870760195 scopus 로고    scopus 로고
    • Protein translocation across the rough endoplasmic reticulum
    • Mandon, E.C., S.F. Trueman, and R. Gilmore. 2013. Protein translocation across the rough endoplasmic reticulum. Cold Spring Harb. Perspect. Biol. 5:a013342. http://dx.doi.org/10.1101/cshperspect.a013342
    • (2013) Cold Spring Harb. Perspect. Biol , vol.5
    • Mandon, E.C.1    Trueman, S.F.2    Gilmore, R.3
  • 35
    • 84891347210 scopus 로고    scopus 로고
    • Der1 promotes movement of misfolded proteins through the endoplasmic reticulum membrane
    • Mehnert, M., T. Sommer, and E. Jarosch. 2014. Der1 promotes movement of misfolded proteins through the endoplasmic reticulum membrane. Nat. Cell Biol. 16:77-86. http://dx.doi.org/10.1038/ncb2882
    • (2014) Nat. Cell Biol , vol.16 , pp. 77-86
    • Mehnert, M.1    Sommer, T.2    Jarosch, E.3
  • 36
    • 37649025515 scopus 로고    scopus 로고
    • Dissecting the ER-associated degradation of a misfolded polytopic membrane protein
    • Nakatsukasa, K., G. Huyer, S. Michaelis, and J.L. Brodsky. 2008. Dissecting the ER-associated degradation of a misfolded polytopic membrane protein. Cell. 132:101-112. http://dx.doi.org/10.1016/j.cell.2007.11.023
    • (2008) Cell , vol.132 , pp. 101-112
    • Nakatsukasa, K.1    Huyer, G.2    Michaelis, S.3    Brodsky, J.L.4
  • 37
    • 67349172917 scopus 로고    scopus 로고
    • The trafficking and regulation of membrane receptors by the RING-CH ubiquitin E3 ligases
    • Nathan, J.A., and P.J. Lehner. 2009. The trafficking and regulation of membrane receptors by the RING-CH ubiquitin E3 ligases. Exp. Cell Res. 315:1593-1600. http://dx.doi.org/10.1016/j.yexcr.2008.10.026
    • (2009) Exp. Cell Res , vol.315 , pp. 1593-1600
    • Nathan, J.A.1    Lehner, P.J.2
  • 38
    • 0028997459 scopus 로고
    • Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p
    • Panzner, S., L. Dreier, E. Hartmann, S. Kostka, and T.A. Rapoport. 1995. Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p. Cell. 81:561-570. http://dx.doi.org/10.1016/0092-8674(95)90077-2
    • (1995) Cell , vol.81 , pp. 561-570
    • Panzner, S.1    Dreier, L.2    Hartmann, E.3    Kostka, S.4    Rapoport, T.A.5
  • 39
    • 84861361690 scopus 로고    scopus 로고
    • Mechanisms of Sec61/SecY-mediated protein translocation across membranes
    • Park, E., and T.A. Rapoport. 2012. Mechanisms of Sec61/SecY-mediated protein translocation across membranes. Annu Rev Biophys. 41:21-40. http://dx.doi.org/10.1146/annurev-biophys-050511-102312
    • (2012) Annu Rev Biophys , vol.41 , pp. 21-40
    • Park, E.1    Rapoport, T.A.2
  • 40
    • 32544437041 scopus 로고    scopus 로고
    • Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways
    • Ravid, T., S.G. Kreft, and M. Hochstrasser. 2006. Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways. EMBO J. 25:533-543. http://dx.doi.org/10.1038/sj.emboj.7600946
    • (2006) EMBO J , vol.25 , pp. 533-543
    • Ravid, T.1    Kreft, S.G.2    Hochstrasser, M.3
  • 41
    • 84864022349 scopus 로고    scopus 로고
    • Aberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase
    • Rubenstein, E.M., S.G. Kreft, W. Greenblatt, R. Swanson, and M. Hochstrasser. 2012. Aberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase. J. Cell Biol. 197:761-773. http://dx.doi.org/10.1083/jcb.201203061
    • (2012) J. Cell Biol , vol.197 , pp. 761-773
    • Rubenstein, E.M.1    Kreft, S.G.2    Greenblatt, W.3    Swanson, R.4    Hochstrasser, M.5
  • 42
    • 84896270715 scopus 로고    scopus 로고
    • Quality control: ER-associated degradation: protein quality control and beyond
    • Ruggiano, A., O. Foresti, and P. Carvalho. 2014. Quality control: ER-associated degradation: protein quality control and beyond. J. Cell Biol. 204:869-879.
    • (2014) J. Cell Biol , vol.204 , pp. 869-879
    • Ruggiano, A.1    Foresti, O.2    Carvalho, P.3
  • 43
    • 64749087257 scopus 로고    scopus 로고
    • Misfolded membrane proteins are specifically recognized by the transmembrane domain of the Hrd1p ubiquitin ligase
    • Sato, B.K., D. Schulz, P.H. Do, and R.Y. Hampton. 2009. Misfolded membrane proteins are specifically recognized by the transmembrane domain of the Hrd1p ubiquitin ligase. Mol. Cell. 34:212-222. http://dx.doi.org/10.1016/j.molcel.2009.03.010
    • (2009) Mol. Cell , vol.34 , pp. 212-222
    • Sato, B.K.1    Schulz, D.2    Do, P.H.3    Hampton, R.Y.4
  • 44
  • 45
    • 80054041334 scopus 로고    scopus 로고
    • Membrane protein insertion at the endoplasmic reticulum
    • Shao, S., and R.S. Hegde. 2011. Membrane protein insertion at the endoplasmic reticulum. Annu. Rev. Cell Dev. Biol. 27:25-56. http://dx.doi.org/10.1146/annurev-cellbio-092910-154125
    • (2011) Annu. Rev. Cell Dev. Biol , vol.27 , pp. 25-56
    • Shao, S.1    Hegde, R.S.2
  • 46
    • 84884308471 scopus 로고    scopus 로고
    • Previously unknown role for the ubiquitin ligase Ubr1 in endoplasmic reticulum-associated protein degradation
    • Stolz, A., S. Besser, H. Hottmann, and D.H. Wolf. 2013. Previously unknown role for the ubiquitin ligase Ubr1 in endoplasmic reticulum-associated protein degradation. Proc. Natl. Acad. Sci. USA. 110:15271-15276. http://dx.doi.org/10.1073/pnas.1304928110
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 15271-15276
    • Stolz, A.1    Besser, S.2    Hottmann, H.3    Wolf, D.H.4
  • 47
    • 84867116845 scopus 로고    scopus 로고
    • Split-Doa10: a naturally split polytopic eukaryotic membrane protein generated by fission of a nuclear gene
    • Stuerner, E., S. Kuraku, M. Hochstrasser, and S.G. Kreft. 2012. Split-Doa10: a naturally split polytopic eukaryotic membrane protein generated by fission of a nuclear gene. PLoS ONE. 7:e45194. http://dx.doi.org/10.1371/journal.pone.0045194
    • (2012) PLoS ONE , vol.7
    • Stuerner, E.1    Kuraku, S.2    Hochstrasser, M.3    Kreft, S.G.4
  • 48
    • 0035887277 scopus 로고    scopus 로고
    • A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matα2 repressor degradation
    • Swanson, R., M. Locher, and M. Hochstrasser. 2001. A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matα2 repressor degradation. Genes Dev. 15:2660-2674. http://dx.doi.org/10.1101/gad.933301
    • (2001) Genes Dev , vol.15 , pp. 2660-2674
    • Swanson, R.1    Locher, M.2    Hochstrasser, M.3
  • 49
    • 0029937560 scopus 로고    scopus 로고
    • Yeast protein translocation complex: isolation of two genes SEB1 and SEB2 encoding proteins homologous to the Sec61 β subunit
    • Toikkanen, J., E. Gatti, K. Takei, M. Saloheimo, V.M. Olkkonen, H. Söderlund, P. De Camilli, and S. Keränen. 1996. Yeast protein translocation complex: isolation of two genes SEB1 and SEB2 encoding proteins homologous to the Sec61 β subunit. Yeast. 12:425-438. http://dx.doi.org/10.1002/(SICI)1097-0061(199604)12:5<425::AID-YEA924>3.0.CO;2-B
    • (1996) Yeast , vol.12 , pp. 425-438
    • Toikkanen, J.1    Gatti, E.2    Takei, K.3    Saloheimo, M.4    Olkkonen, V.M.5    Söderlund, H.6    De Camilli, P.7    Keränen, S.8
  • 51
    • 0026068805 scopus 로고
    • Naming a targeting signal
    • Varshavsky, A. 1991. Naming a targeting signal. Cell. 64:13-15. http://dx.doi.org/10.1016/0092-8674(91)90202-A
    • (1991) Cell , vol.64 , pp. 13-15
    • Varshavsky, A.1
  • 52
    • 2442451126 scopus 로고    scopus 로고
    • Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control
    • Vashist, S., and D.T. Ng. 2004. Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control. J. Cell Biol. 165:41-52. http://dx.doi.org/10.1083/jcb.200309132
    • (2004) J. Cell Biol , vol.165 , pp. 41-52
    • Vashist, S.1    Ng, D.T.2
  • 53
    • 56749176947 scopus 로고    scopus 로고
    • One step at a time: endoplasmic reticulum-associated degradation
    • Vembar, S.S., and J.L. Brodsky. 2008. One step at a time: endoplasmic reticulum-associated degradation. Nat. Rev. Mol. Cell Biol. 9:944-957. http://dx.doi.org/10.1038/nrm2546
    • (2008) Nat. Rev. Mol. Cell Biol , vol.9 , pp. 944-957
    • Vembar, S.S.1    Brodsky, J.L.2
  • 54
    • 0035875921 scopus 로고    scopus 로고
    • Sec61p-independent degradation of the tail-anchored ER membrane protein Ubc6p
    • Walter, J., J. Urban, C. Volkwein, and T. Sommer. 2001. Sec61p-independent degradation of the tail-anchored ER membrane protein Ubc6p. EMBO J. 20: 3124-3131. http://dx.doi.org/10.1093/emboj/20.12.3124
    • (2001) EMBO J , vol.20 , pp. 3124-3131
    • Walter, J.1    Urban, J.2    Volkwein, C.3    Sommer, T.4
  • 55
    • 3543104812 scopus 로고    scopus 로고
    • Model for the interaction of gammaherpesvirus 68 RING-CH finger protein mK3 with major histocompatibility complex class I and the peptideloading complex
    • Wang, X., L. Lybarger, R. Connors, M.R. Harris, and T.H. Hansen. 2004. Model for the interaction of gammaherpesvirus 68 RING-CH finger protein mK3 with major histocompatibility complex class I and the peptideloading complex. J. Virol. 78:8673-8686. http://dx.doi.org/10.1128/JVI.78.16.8673-8686.2004
    • (2004) J. Virol , vol.78 , pp. 8673-8686
    • Wang, X.1    Lybarger, L.2    Connors, R.3    Harris, M.R.4    Hansen, T.H.5
  • 56
    • 56949087771 scopus 로고    scopus 로고
    • Viral and cellular MARCH ubiquitin ligases and cancer
    • Wang, X., R.A. Herr, and T. Hansen. 2008. Viral and cellular MARCH ubiquitin ligases and cancer. Semin. Cancer Biol. 18:441-450. http://dx.doi.org/10.1016/j.semcancer.2008.09.002
    • (2008) Semin. Cancer Biol , vol.18 , pp. 441-450
    • Wang, X.1    Herr, R.A.2    Hansen, T.3
  • 57
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
    • Ye, Y., H.H. Meyer, and T.A. Rapoport. 2001. The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature. 414:652-656. http://dx.doi.org/10.1038/414652a
    • (2001) Nature , vol.414 , pp. 652-656
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 58
    • 84924533915 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation at the yeast endoplasmic reticulum and nuclear envelope
    • Zattas, D., and M. Hochstrasser. 2015. Ubiquitin-dependent protein degradation at the yeast endoplasmic reticulum and nuclear envelope. Crit. Rev. Biochem. Mol. Biol. 50:1-17. http://dx.doi.org/10.3109/10409238.2014.959889
    • (2015) Crit. Rev. Biochem. Mol. Biol , vol.50 , pp. 1-17
    • Zattas, D.1    Hochstrasser, M.2
  • 59
    • 70450242800 scopus 로고    scopus 로고
    • Functional characterization of the trans-membrane domain interactions of the Sec61 protein translocation complex β-subunit
    • Zhao, X., and J. Jäntti. 2009. Functional characterization of the trans-membrane domain interactions of the Sec61 protein translocation complex β-subunit. BMC Cell Biol. 10:76. http://dx.doi.org/10.1186/1471-2121-10-76
    • (2009) BMC Cell Biol , vol.10 , pp. 76
    • Zhao, X.1    Jäntti, J.2


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