메뉴 건너뛰기




Volumn 23, Issue 5, 2012, Pages 530-537

Selective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradation

Author keywords

Degradation; Misfolded protein; Proteasome; Ubiquitin

Indexed keywords

MEMBRANE PROTEIN; MITOCHONDRIAL UBIQUITIN PROTEIN LIGASE; PARKIN; PROTEIN DOA10; PROTEIN HRD1; PROTEIN HUL5; PROTEIN LTN1; PROTEIN RKR1; PROTEIN SAN1; PROTEIN SLX5; PROTEIN UBR1; UBIQUITIN; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 84863723691     PISSN: 10849521     EISSN: 10963634     Source Type: Journal    
DOI: 10.1016/j.semcdb.2011.12.006     Document Type: Review
Times cited : (54)

References (124)
  • 1
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • Balch W.E., Morimoto R.I., Dillin A., Kelly J.W. Adapting proteostasis for disease intervention. Science 2008, 319(5865):916-919.
    • (2008) Science , vol.319 , Issue.5865 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 2
    • 0033520987 scopus 로고    scopus 로고
    • Posttranslational quality control: folding, refolding, and degrading proteins
    • Wickner S., Maurizi M.R., Gottesman S. Posttranslational quality control: folding, refolding, and degrading proteins. Science 1999, 286(5446):1888-1893.
    • (1999) Science , vol.286 , Issue.5446 , pp. 1888-1893
    • Wickner, S.1    Maurizi, M.R.2    Gottesman, S.3
  • 3
    • 77954955686 scopus 로고    scopus 로고
    • Heat shock factors: integrators of cell stress, development and lifespan
    • Akerfelt M., Morimoto R.I., Sistonen L. Heat shock factors: integrators of cell stress, development and lifespan. Nat Rev Mol Cell Biol 2010, 11(8):545-555.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , Issue.8 , pp. 545-555
    • Akerfelt, M.1    Morimoto, R.I.2    Sistonen, L.3
  • 4
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron D., Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol 2007, 8(7):519-529.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , Issue.7 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 5
    • 77955844171 scopus 로고    scopus 로고
    • Chaperone networks: tipping the balance in protein folding diseases
    • Voisine C., Pedersen J.S., Morimoto R.I. Chaperone networks: tipping the balance in protein folding diseases. Neurobiol Dis 2010, 40(1):12-20.
    • (2010) Neurobiol Dis , vol.40 , Issue.1 , pp. 12-20
    • Voisine, C.1    Pedersen, J.S.2    Morimoto, R.I.3
  • 6
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl F.U., Bracher A., Hayer-Hartl M. Molecular chaperones in protein folding and proteostasis. Nature 2011, 475(7356):324-332.
    • (2011) Nature , vol.475 , Issue.7356 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 7
    • 79951762136 scopus 로고    scopus 로고
    • How budding yeast sense and transduce the oxidative stress signal and the impact in cell growth and morphogenesis
    • de la Torre-Ruiz M.A., Mozo-Villarias A., Pujol N., Petkova M.I. How budding yeast sense and transduce the oxidative stress signal and the impact in cell growth and morphogenesis. Curr Protein Pept Sci 2010, 11(8):669-679.
    • (2010) Curr Protein Pept Sci , vol.11 , Issue.8 , pp. 669-679
    • de la Torre-Ruiz, M.A.1    Mozo-Villarias, A.2    Pujol, N.3    Petkova, M.I.4
  • 8
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction
    • Glickman M.H., Ciechanover A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev 2002, 82(2):373-428.
    • (2002) Physiol Rev , vol.82 , Issue.2 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 9
    • 50149086108 scopus 로고    scopus 로고
    • Diversity of degradation signals in the ubiquitin-proteasome system
    • Ravid T., Hochstrasser M. Diversity of degradation signals in the ubiquitin-proteasome system. Nat Rev Mol Cell Biol 2008, 9(9):679-690.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , Issue.9 , pp. 679-690
    • Ravid, T.1    Hochstrasser, M.2
  • 10
    • 11244351579 scopus 로고    scopus 로고
    • Function and regulation of cullin-RING ubiquitin ligases
    • Petroski M.D., Deshaies R.J. Function and regulation of cullin-RING ubiquitin ligases. Nat Rev Mol Cell Biol 2005, 6(1):9-20.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , Issue.1 , pp. 9-20
    • Petroski, M.D.1    Deshaies, R.J.2
  • 11
    • 0031885043 scopus 로고    scopus 로고
    • Der3p/Hrd1p is required for endoplasmic reticulum-associated degradation of misfolded lumenal and integral membrane proteins
    • Bordallo J., Plemper R.K., Finger A., Wolf D.H. Der3p/Hrd1p is required for endoplasmic reticulum-associated degradation of misfolded lumenal and integral membrane proteins. Mol Biol Cell 1998, 9(1):209-222.
    • (1998) Mol Biol Cell , vol.9 , Issue.1 , pp. 209-222
    • Bordallo, J.1    Plemper, R.K.2    Finger, A.3    Wolf, D.H.4
  • 12
    • 0029811218 scopus 로고    scopus 로고
    • Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein
    • Hampton R.Y., Gardner R.G., Rine J. Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein. Mol Biol Cell 1996, 7(12):2029-2044.
    • (1996) Mol Biol Cell , vol.7 , Issue.12 , pp. 2029-2044
    • Hampton, R.Y.1    Gardner, R.G.2    Rine, J.3
  • 13
    • 0034597161 scopus 로고    scopus 로고
    • Endoplasmic reticulum degradation requires lumen to cytosol signaling. Transmembrane control of Hrd1p by Hrd3p
    • Gardner R.G., Swarbrick G.M., Bays N.W., Cronin S.R., Wilhovsky S., Seelig L., et al. Endoplasmic reticulum degradation requires lumen to cytosol signaling. Transmembrane control of Hrd1p by Hrd3p. J Cell Biol 2000, 151(1):69-82.
    • (2000) J Cell Biol , vol.151 , Issue.1 , pp. 69-82
    • Gardner, R.G.1    Swarbrick, G.M.2    Bays, N.W.3    Cronin, S.R.4    Wilhovsky, S.5    Seelig, L.6
  • 14
    • 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., Wolf D.H. Membrane topology and function of Der3/Hrd1p as a ubiquitin-protein ligase (E3) involved in endoplasmic reticulum degradation. J Biol Chem 2001, 276(14):10663-10669.
    • (2001) J Biol Chem , vol.276 , Issue.14 , pp. 10663-10669
    • Deak, P.M.1    Wolf, D.H.2
  • 15
    • 0035807839 scopus 로고    scopus 로고
    • The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum
    • Fang S., Ferrone M., Yang C., Jensen J.P., Tiwari S., Weissman A.M. The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum. Proc Natl Acad Sci USA 2001, 98(25):14422-14427.
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.25 , pp. 14422-14427
    • Fang, S.1    Ferrone, M.2    Yang, C.3    Jensen, J.P.4    Tiwari, S.5    Weissman, A.M.6
  • 16
    • 0037021416 scopus 로고    scopus 로고
    • Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation
    • Kaneko M., Ishiguro M., Niinuma Y., Uesugi M., Nomura Y. Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation. FEBS Lett 2002, 532(1-2):147-152.
    • (2002) FEBS Lett , vol.532 , Issue.1-2 , pp. 147-152
    • Kaneko, M.1    Ishiguro, M.2    Niinuma, Y.3    Uesugi, M.4    Nomura, Y.5
  • 17
    • 34248160996 scopus 로고    scopus 로고
    • The RBCC gene RFP2 (Leu5) encodes a novel transmembrane E3 ubiquitin ligase involved in ERAD
    • Lerner M., Corcoran M., Cepeda D., Nielsen M.L., Zubarev R., Ponten F., et al. The RBCC gene RFP2 (Leu5) encodes a novel transmembrane E3 ubiquitin ligase involved in ERAD. Mol Biol Cell 2007, 18(5):1670-1682.
    • (2007) Mol Biol Cell , vol.18 , Issue.5 , pp. 1670-1682
    • Lerner, M.1    Corcoran, M.2    Cepeda, D.3    Nielsen, M.L.4    Zubarev, R.5    Ponten, F.6
  • 19
    • 9144239817 scopus 로고    scopus 로고
    • Human HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulum
    • Kikkert M., Doolman R., Dai M., Avner R., Hassink G., van Voorden S., et al. Human HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulum. J Biol Chem 2004, 279(5):3525-3534.
    • (2004) J Biol Chem , vol.279 , Issue.5 , pp. 3525-3534
    • Kikkert, M.1    Doolman, R.2    Dai, M.3    Avner, R.4    Hassink, G.5    van Voorden, S.6
  • 20
    • 0030660267 scopus 로고    scopus 로고
    • Ubiquitin-mediated regulation of 3-hydroxy-3-methylglutaryl-CoA reductase
    • Hampton R.Y., Bhakta H. Ubiquitin-mediated regulation of 3-hydroxy-3-methylglutaryl-CoA reductase. Proc Natl Acad Sci USA 1997, 94(24):12944-12948.
    • (1997) Proc Natl Acad Sci USA , vol.94 , Issue.24 , pp. 12944-12948
    • Hampton, R.Y.1    Bhakta, H.2
  • 21
    • 0033780610 scopus 로고    scopus 로고
    • A regulatory link between ER-associated protein degradation and the unfolded-protein response
    • Friedlander R., Jarosch E., Urban J., Volkwein C., Sommer T. A regulatory link between ER-associated protein degradation and the unfolded-protein response. Nat Cell Biol 2000, 2(7):379-384.
    • (2000) Nat Cell Biol , vol.2 , Issue.7 , pp. 379-384
    • Friedlander, R.1    Jarosch, E.2    Urban, J.3    Volkwein, C.4    Sommer, T.5
  • 22
    • 0035144199 scopus 로고    scopus 로고
    • Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation
    • Bays N.W., Gardner R.G., Seelig L.P., Joazeiro C.A., Hampton R.Y. Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation. Nat Cell Biol 2001, 3(1):24-29.
    • (2001) Nat Cell Biol , vol.3 , Issue.1 , pp. 24-29
    • Bays, N.W.1    Gardner, R.G.2    Seelig, L.P.3    Joazeiro, C.A.4    Hampton, R.Y.5
  • 23
    • 0030666729 scopus 로고    scopus 로고
    • Role of Cue1p in ubiquitination and degradation at the ER surface
    • Biederer T., Volkwein C., Sommer T. Role of Cue1p in ubiquitination and degradation at the ER surface. Science 1997, 278(5344):1806-1809.
    • (1997) Science , vol.278 , Issue.5344 , pp. 1806-1809
    • Biederer, T.1    Volkwein, C.2    Sommer, T.3
  • 24
    • 31044437051 scopus 로고    scopus 로고
    • The activity of a human endoplasmic reticulum-associated degradation E3, gp78, requires its Cue domain, RING finger, and an E2-binding site
    • Chen B., Mariano J., Tsai Y.C., Chan A.H., Cohen M., Weissman A.M. The activity of a human endoplasmic reticulum-associated degradation E3, gp78, requires its Cue domain, RING finger, and an E2-binding site. Proc Natl Acad Sci USA 2006, 103(2):341-346.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.2 , pp. 341-346
    • Chen, B.1    Mariano, J.2    Tsai, Y.C.3    Chan, A.H.4    Cohen, M.5    Weissman, A.M.6
  • 25
    • 26244431960 scopus 로고    scopus 로고
    • Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane
    • Lilley B.N., Ploegh H.L. Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane. Proc Natl Acad Sci USA 2005, 102(40):14296-14301.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.40 , pp. 14296-14301
    • Lilley, B.N.1    Ploegh, H.L.2
  • 26
    • 33750359201 scopus 로고    scopus 로고
    • SEL1L, the homologue of yeast Hrd3p, is involved in protein dislocation from the mammalian ER
    • Mueller B., Lilley B.N., Ploegh H.L. SEL1L, the homologue of yeast Hrd3p, is involved in protein dislocation from the mammalian ER. J Cell Biol 2006, 175(2):261-270.
    • (2006) J Cell Biol , vol.175 , Issue.2 , pp. 261-270
    • Mueller, B.1    Lilley, B.N.2    Ploegh, H.L.3
  • 27
    • 0033492290 scopus 로고    scopus 로고
    • Genetic interactions of Hrd3p and Der3p/Hrd1p with Sec61p suggest a retro-translocation complex mediating protein transport for ER degradation
    • Plemper R.K., Bordallo J., Deak P.M., Taxis C., Hitt R., Wolf D.H. Genetic interactions of Hrd3p and Der3p/Hrd1p with Sec61p suggest a retro-translocation complex mediating protein transport for ER degradation. J Cell Sci 1999, 112(Pt 22):4123-4134.
    • (1999) J Cell Sci , vol.112 , Issue.PART 22 , pp. 4123-4134
    • Plemper, R.K.1    Bordallo, J.2    Deak, P.M.3    Taxis, C.4    Hitt, R.5    Wolf, D.H.6
  • 28
    • 33646552435 scopus 로고    scopus 로고
    • The Hrd1p ligase complex forms a linchpin between ER-lumenal substrate selection and Cdc48p recruitment
    • Gauss R., Sommer T., Jarosch E. The Hrd1p ligase complex forms a linchpin between ER-lumenal substrate selection and Cdc48p recruitment. EMBO J 2006, 25(9):1827-1835.
    • (2006) EMBO J , vol.25 , Issue.9 , pp. 1827-1835
    • Gauss, R.1    Sommer, T.2    Jarosch, E.3
  • 29
    • 28144436887 scopus 로고    scopus 로고
    • The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway
    • Schulze A., Standera S., Buerger E., Kikkert M., van Voorden S., Wiertz E., et al. The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway. J Mol Biol 2005, 354(5):1021-1027.
    • (2005) J Mol Biol , vol.354 , Issue.5 , pp. 1021-1027
    • Schulze, A.1    Standera, S.2    Buerger, E.3    Kikkert, M.4    van Voorden, S.5    Wiertz, E.6
  • 30
    • 36249022750 scopus 로고    scopus 로고
    • Characterization of an ERAD pathway for nonglycosylated BiP substrates, which require Herp
    • Okuda-Shimizu Y., Hendershot L.M. Characterization of an ERAD pathway for nonglycosylated BiP substrates, which require Herp. Mol Cell 2007, 28(4):544-554.
    • (2007) Mol Cell , vol.28 , Issue.4 , pp. 544-554
    • Okuda-Shimizu, Y.1    Hendershot, L.M.2
  • 31
    • 70449558838 scopus 로고    scopus 로고
    • Usa1 protein facilitates substrate ubiquitylation through two separate domains
    • Kim I., Li Y., Muniz P., Rao H. Usa1 protein facilitates substrate ubiquitylation through two separate domains. PLoS One 2009, 4(10):e7604.
    • (2009) PLoS One , vol.4 , Issue.10
    • Kim, I.1    Li, Y.2    Muniz, P.3    Rao, H.4
  • 33
    • 77949312283 scopus 로고    scopus 로고
    • Usa1p is required for optimal function and regulation of the Hrd1p endoplasmic reticulum-associated degradation ubiquitin ligase
    • Carroll S.M., Hampton R.Y. Usa1p is required for optimal function and regulation of the Hrd1p endoplasmic reticulum-associated degradation ubiquitin ligase. J Biol Chem 2010, 285(8):5146-5156.
    • (2010) J Biol Chem , vol.285 , Issue.8 , pp. 5146-5156
    • Carroll, S.M.1    Hampton, R.Y.2
  • 34
    • 33746228127 scopus 로고    scopus 로고
    • Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins
    • Carvalho P., Goder V., Rapoport T.A. Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins. Cell 2006, 126(2):361-373.
    • (2006) Cell , vol.126 , Issue.2 , pp. 361-373
    • Carvalho, P.1    Goder, V.2    Rapoport, T.A.3
  • 35
    • 64749087257 scopus 로고    scopus 로고
    • Misfolded membrane proteins are specifically recognized by the transmembrane domain of the Hrd1p ubiquitin ligase
    • Sato B.K., Schulz D., Do P.H., Hampton R.Y. Misfolded membrane proteins are specifically recognized by the transmembrane domain of the Hrd1p ubiquitin ligase. Mol Cell 2009, 34(2):212-222.
    • (2009) Mol Cell , vol.34 , Issue.2 , pp. 212-222
    • Sato, B.K.1    Schulz, D.2    Do, P.H.3    Hampton, R.Y.4
  • 36
    • 0030041781 scopus 로고    scopus 로고
    • A novel protein specifically required for endoplasmic reticulum degradation in yeast
    • Knop M., Finger A., Braun T., Hellmuth K., Der1 Wolf D.H. a novel protein specifically required for endoplasmic reticulum degradation in yeast. EMBO J 1996, 15(4):753-763.
    • (1996) EMBO J , vol.15 , Issue.4 , pp. 753-763
    • Knop, M.1    Finger, A.2    Braun, T.3    Hellmuth, K.4    Der1, W.D.H.5
  • 37
    • 3042616595 scopus 로고    scopus 로고
    • A membrane protein required for dislocation of misfolded proteins from the ER
    • Lilley B.N., Ploegh H.L. A membrane protein required for dislocation of misfolded proteins from the ER. Nature 2004, 429(6994):834-840.
    • (2004) Nature , vol.429 , Issue.6994 , pp. 834-840
    • Lilley, B.N.1    Ploegh, H.L.2
  • 38
    • 3042677637 scopus 로고    scopus 로고
    • A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol
    • Ye Y., Shibata Y., Yun C., Ron D., Rapoport T.A. A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol. Nature 2004, 429(6994):841-847.
    • (2004) Nature , vol.429 , Issue.6994 , pp. 841-847
    • Ye, Y.1    Shibata, Y.2    Yun, C.3    Ron, D.4    Rapoport, T.A.5
  • 39
    • 80455164551 scopus 로고    scopus 로고
    • Derlin-1 is a rhomboid pseudoprotease required for the dislocation of mutant alpha-1 antitrypsin from the endoplasmic reticulum
    • Greenblatt E.J., Olzmann J.A., Kopito R.R. Derlin-1 is a rhomboid pseudoprotease required for the dislocation of mutant alpha-1 antitrypsin from the endoplasmic reticulum. Nat Struct Mol Biol 2011, 18(10):1147-1152.
    • (2011) Nat Struct Mol Biol , vol.18 , Issue.10 , pp. 1147-1152
    • Greenblatt, E.J.1    Olzmann, J.A.2    Kopito, R.R.3
  • 40
    • 1842409617 scopus 로고    scopus 로고
    • Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation
    • Plemper R.K., Bohmler S., Bordallo J., Sommer T., Wolf D.H. Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature 1997, 388(6645):891-895.
    • (1997) Nature , vol.388 , Issue.6645 , pp. 891-895
    • Plemper, R.K.1    Bohmler, S.2    Bordallo, J.3    Sommer, T.4    Wolf, D.H.5
  • 41
    • 0030976048 scopus 로고    scopus 로고
    • Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries
    • Rudiger S., Germeroth L., Schneider-Mergener J., Bukau B. Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries. EMBO J 1997, 16(7):1501-1507.
    • (1997) EMBO J , vol.16 , Issue.7 , pp. 1501-1507
    • Rudiger, S.1    Germeroth, L.2    Schneider-Mergener, J.3    Bukau, B.4
  • 42
    • 24944478240 scopus 로고    scopus 로고
    • Yos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD
    • Szathmary R., Bielmann R., Nita-Lazar M., Burda P., Jakob C.A. Yos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD. Mol Cell 2005, 19(6):765-775.
    • (2005) Mol Cell , vol.19 , Issue.6 , pp. 765-775
    • Szathmary, R.1    Bielmann, R.2    Nita-Lazar, M.3    Burda, P.4    Jakob, C.A.5
  • 43
    • 24944552879 scopus 로고    scopus 로고
    • Yos9p detects and targets misfolded glycoproteins for ER-associated degradation
    • Kim W., Spear E.D., Ng D.T. Yos9p detects and targets misfolded glycoproteins for ER-associated degradation. Mol Cell 2005, 19(6):753-764.
    • (2005) Mol Cell , vol.19 , Issue.6 , pp. 753-764
    • Kim, W.1    Spear, E.D.2    Ng, D.T.3
  • 44
    • 24944583185 scopus 로고    scopus 로고
    • Exploration of the topological requirements of ERAD identifies Yos9p as a lectin sensor of misfolded glycoproteins in the ER lumen
    • Bhamidipati A., Denic V., Quan E.M., Weissman J.S. Exploration of the topological requirements of ERAD identifies Yos9p as a lectin sensor of misfolded glycoproteins in the ER lumen. Mol Cell 2005, 19(6):741-751.
    • (2005) Mol Cell , vol.19 , Issue.6 , pp. 741-751
    • Bhamidipati, A.1    Denic, V.2    Quan, E.M.3    Weissman, J.S.4
  • 45
    • 8844270968 scopus 로고    scopus 로고
    • A genome-wide screen identifies Yos9p as essential for ER-associated degradation of glycoproteins
    • Buschhorn B.A., Kostova Z., Medicherla B., Wolf D.H. A genome-wide screen identifies Yos9p as essential for ER-associated degradation of glycoproteins. FEBS Lett 2004, 577(3):422-426.
    • (2004) FEBS Lett , vol.577 , Issue.3 , pp. 422-426
    • Buschhorn, B.A.1    Kostova, Z.2    Medicherla, B.3    Wolf, D.H.4
  • 46
    • 40249088336 scopus 로고    scopus 로고
    • OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD
    • Christianson J.C., Shaler T.A., Tyler R.E., Kopito R.R. OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD. Nat Cell Biol 2008, 10(3):272-282.
    • (2008) Nat Cell Biol , vol.10 , Issue.3 , pp. 272-282
    • Christianson, J.C.1    Shaler, T.A.2    Tyler, R.E.3    Kopito, R.R.4
  • 47
    • 33746587049 scopus 로고    scopus 로고
    • A complex of Yos9p and the HRD ligase integrates endoplasmic reticulum quality control into the degradation machinery
    • Gauss R., Jarosch E., Sommer T., Hirsch C. A complex of Yos9p and the HRD ligase integrates endoplasmic reticulum quality control into the degradation machinery. Nat Cell Biol 2006, 8(8):849-854.
    • (2006) Nat Cell Biol , vol.8 , Issue.8 , pp. 849-854
    • Gauss, R.1    Jarosch, E.2    Sommer, T.3    Hirsch, C.4
  • 48
    • 33746208871 scopus 로고    scopus 로고
    • A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation
    • Denic V., Quan E.M., Weissman J.S. A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation. Cell 2006, 126(2):349-359.
    • (2006) Cell , vol.126 , Issue.2 , pp. 349-359
    • Denic, V.1    Quan, E.M.2    Weissman, J.S.3
  • 49
    • 67650535999 scopus 로고    scopus 로고
    • Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans
    • Hosokawa N., Kamiya Y., Kamiya D., Kato K., Nagata K. Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans. J Biol Chem 2009, 284(25):17061-17068.
    • (2009) J Biol Chem , vol.284 , Issue.25 , pp. 17061-17068
    • Hosokawa, N.1    Kamiya, Y.2    Kamiya, D.3    Kato, K.4    Nagata, K.5
  • 50
    • 57749083532 scopus 로고    scopus 로고
    • Defining the glycan destruction signal for endoplasmic reticulum-associated degradation
    • Quan E.M., Kamiya Y., Kamiya D., Denic V., Weibezahn J., Kato K., et al. Defining the glycan destruction signal for endoplasmic reticulum-associated degradation. Mol Cell 2008, 32(6):870-877.
    • (2008) Mol Cell , vol.32 , Issue.6 , pp. 870-877
    • Quan, E.M.1    Kamiya, Y.2    Kamiya, D.3    Denic, V.4    Weibezahn, J.5    Kato, K.6
  • 51
    • 67749101849 scopus 로고    scopus 로고
    • Intrinsic conformational determinants signal protein misfolding to the Hrd1/Htm1 endoplasmic reticulum-associated degradation system
    • Xie W., Kanehara K., Sayeed A., Ng D.T. Intrinsic conformational determinants signal protein misfolding to the Hrd1/Htm1 endoplasmic reticulum-associated degradation system. Mol Biol Cell 2009, 20(14):3317-3329.
    • (2009) Mol Biol Cell , vol.20 , Issue.14 , pp. 3317-3329
    • Xie, W.1    Kanehara, K.2    Sayeed, A.3    Ng, D.T.4
  • 52
    • 17844382159 scopus 로고    scopus 로고
    • Importance of carbohydrate positioning in the recognition of mutated CPY for ER-associated degradation
    • Kostova Z., Wolf D.H. Importance of carbohydrate positioning in the recognition of mutated CPY for ER-associated degradation. J Cell Sci 2005, 118(Pt 7):1485-1492.
    • (2005) J Cell Sci , vol.118 , Issue.PART 7 , pp. 1485-1492
    • Kostova, Z.1    Wolf, D.H.2
  • 53
    • 17644414638 scopus 로고    scopus 로고
    • Single, context-specific glycans can target misfolded glycoproteins for ER-associated degradation
    • Spear E.D., Ng D.T. Single, context-specific glycans can target misfolded glycoproteins for ER-associated degradation. J Cell Biol 2005, 169(1):73-82.
    • (2005) J Cell Biol , vol.169 , Issue.1 , pp. 73-82
    • Spear, E.D.1    Ng, D.T.2
  • 54
    • 80053285187 scopus 로고    scopus 로고
    • A control protein for misfolded glycosylated and non-glycosylated proteins in ERAD
    • Benitez E.M., Stolz A., Yos9 Wolf D.H. a control protein for misfolded glycosylated and non-glycosylated proteins in ERAD. FEBS Lett 2011, 585(19):3015-3019.
    • (2011) FEBS Lett , vol.585 , Issue.19 , pp. 3015-3019
    • Benitez, E.M.1    Stolz, A.2    Yos9, W.D.H.3
  • 55
    • 80051673589 scopus 로고    scopus 로고
    • Yos9p assists in the degradation of certain non-glycosylated proteins from the endoplasmic reticulum
    • Jaenicke L.A., Brendebach H., Selbach M., Hirsch C. Yos9p assists in the degradation of certain non-glycosylated proteins from the endoplasmic reticulum. Mol Biol Cell 2011.
    • (2011) Mol Biol Cell
    • Jaenicke, L.A.1    Brendebach, H.2    Selbach, M.3    Hirsch, C.4
  • 56
    • 0035887277 scopus 로고    scopus 로고
    • A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation
    • Swanson R., Locher M., Hochstrasser M. A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation. Genes Dev 2001, 15(20):2660-2674.
    • (2001) Genes Dev , vol.15 , Issue.20 , pp. 2660-2674
    • Swanson, R.1    Locher, M.2    Hochstrasser, M.3
  • 57
    • 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., Piluek W.F., Fansler Z., Kreft S.G., Hochstrasser M., Brodsky J.L., et al. 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 2004, 279(37):38369-38378.
    • (2004) J Biol Chem , vol.279 , Issue.37 , pp. 38369-38378
    • Huyer, G.1    Piluek, W.F.2    Fansler, Z.3    Kreft, S.G.4    Hochstrasser, M.5    Brodsky, J.L.6
  • 58
    • 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., Wang L., Hochstrasser M. Membrane topology of the yeast endoplasmic reticulum-localized ubiquitin ligase Doa10 and comparison with its human ortholog TEB4 (MARCH-VI). J Biol Chem 2006, 281(8):4646-4653.
    • (2006) J Biol Chem , vol.281 , Issue.8 , pp. 4646-4653
    • Kreft, S.G.1    Wang, L.2    Hochstrasser, M.3
  • 59
    • 70349316465 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase TEB4 mediates degradation of type 2 iodothyronine deiodinase
    • Zavacki A.M., Arrojo E.D.R., Freitas B.C., Chung M., Harney J.W., Egri P., et al. The E3 ubiquitin ligase TEB4 mediates degradation of type 2 iodothyronine deiodinase. Mol Cell Biol 2009, 29(19):5339-5347.
    • (2009) Mol Cell Biol , vol.29 , Issue.19 , pp. 5339-5347
    • Zavacki, A.M.1    Arrojo, E.D.R.2    Freitas, B.C.3    Chung, M.4    Harney, J.W.5    Egri, P.6
  • 60
    • 32544437041 scopus 로고    scopus 로고
    • Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways
    • Ravid T., Kreft S.G., Hochstrasser M. Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways. EMBO J 2006, 25(3):533-543.
    • (2006) EMBO J , vol.25 , Issue.3 , pp. 533-543
    • Ravid, T.1    Kreft, S.G.2    Hochstrasser, M.3
  • 61
    • 77951218298 scopus 로고    scopus 로고
    • Ubiquitin chain elongation enzyme Ufd2 regulates a subset of Doa10 substrates
    • Liu C., van Dyk D., Xu P., Choe V., Pan H., Peng J., et al. Ubiquitin chain elongation enzyme Ufd2 regulates a subset of Doa10 substrates. J Biol Chem 2010, 285(14):10265-10272.
    • (2010) J Biol Chem , vol.285 , Issue.14 , pp. 10265-10272
    • Liu, C.1    van Dyk, D.2    Xu, P.3    Choe, V.4    Pan, H.5    Peng, J.6
  • 62
    • 0032563319 scopus 로고    scopus 로고
    • Degradation signal masking by heterodimerization of MATalpha2 and MATa1 blocks their mutual destruction by the ubiquitin-proteasome pathway
    • Johnson P.R., Swanson R., Rakhilina L., Hochstrasser M. Degradation signal masking by heterodimerization of MATalpha2 and MATa1 blocks their mutual destruction by the ubiquitin-proteasome pathway. Cell 1998, 94(2):217-227.
    • (1998) Cell , vol.94 , Issue.2 , pp. 217-227
    • Johnson, P.R.1    Swanson, R.2    Rakhilina, L.3    Hochstrasser, M.4
  • 63
    • 57749116223 scopus 로고    scopus 로고
    • Degradation of a cytosolic protein requires endoplasmic reticulum-associated degradation machinery
    • Metzger M.B., Maurer M.J., Dancy B.M., Michaelis S. Degradation of a cytosolic protein requires endoplasmic reticulum-associated degradation machinery. J Biol Chem 2008, 283(47):32302-32316.
    • (2008) J Biol Chem , vol.283 , Issue.47 , pp. 32302-32316
    • Metzger, M.B.1    Maurer, M.J.2    Dancy, B.M.3    Michaelis, S.4
  • 64
    • 0032525130 scopus 로고    scopus 로고
    • Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae
    • Gilon T., Chomsky O., Kulka R.G. Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae. EMBO J 1998, 17(10):2759-2766.
    • (1998) EMBO J , vol.17 , Issue.10 , pp. 2759-2766
    • Gilon, T.1    Chomsky, O.2    Kulka, R.G.3
  • 65
    • 0033834458 scopus 로고    scopus 로고
    • Degradation signals recognized by the Ubc6p-Ubc7p ubiquitin-conjugating enzyme pair
    • Gilon T., Chomsky O., Kulka R.G. Degradation signals recognized by the Ubc6p-Ubc7p ubiquitin-conjugating enzyme pair. Mol Cell Biol 2000, 20(19):7214-7219.
    • (2000) Mol Cell Biol , vol.20 , Issue.19 , pp. 7214-7219
    • Gilon, T.1    Chomsky, O.2    Kulka, R.G.3
  • 66
    • 0036166924 scopus 로고    scopus 로고
    • A transmembrane ubiquitin ligase required to sort membrane proteins into multivesicular bodies
    • Reggiori F., Pelham H.R. A transmembrane ubiquitin ligase required to sort membrane proteins into multivesicular bodies. Nat Cell Biol 2002, 4(2):117-123.
    • (2002) Nat Cell Biol , vol.4 , Issue.2 , pp. 117-123
    • Reggiori, F.1    Pelham, H.R.2
  • 67
    • 1942439642 scopus 로고    scopus 로고
    • Bsd2 binds the ubiquitin ligase Rsp5 and mediates the ubiquitination of transmembrane proteins
    • Hettema E.H., Valdez-Taubas J., Pelham H.R. Bsd2 binds the ubiquitin ligase Rsp5 and mediates the ubiquitination of transmembrane proteins. EMBO J 2004, 23(6):1279-1288.
    • (2004) EMBO J , vol.23 , Issue.6 , pp. 1279-1288
    • Hettema, E.H.1    Valdez-Taubas, J.2    Pelham, H.R.3
  • 68
    • 2342450002 scopus 로고    scopus 로고
    • Ubiquitin-mediated targeting of a mutant plasma membrane ATPase, Pma1-7, to the endosomal/vacuolar system in yeast
    • Pizzirusso M., Chang A. Ubiquitin-mediated targeting of a mutant plasma membrane ATPase, Pma1-7, to the endosomal/vacuolar system in yeast. Mol Biol Cell 2004, 15(5):2401-2409.
    • (2004) Mol Biol Cell , vol.15 , Issue.5 , pp. 2401-2409
    • Pizzirusso, M.1    Chang, A.2
  • 69
    • 50649116818 scopus 로고    scopus 로고
    • Misfolded proteins partition between two distinct quality control compartments
    • Kaganovich D., Kopito R., Frydman J. Misfolded proteins partition between two distinct quality control compartments. Nature 2008, 454(7208):1088-1095.
    • (2008) Nature , vol.454 , Issue.7208 , pp. 1088-1095
    • Kaganovich, D.1    Kopito, R.2    Frydman, J.3
  • 70
    • 0035900793 scopus 로고    scopus 로고
    • CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation
    • Jiang J., Ballinger C.A., Wu Y., Dai Q., Cyr D.M., Hohfeld J., et al. CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation. J Biol Chem 2001, 276(46):42938-42944.
    • (2001) J Biol Chem , vol.276 , Issue.46 , pp. 42938-42944
    • Jiang, J.1    Ballinger, C.A.2    Wu, Y.3    Dai, Q.4    Cyr, D.M.5    Hohfeld, J.6
  • 71
    • 0033013126 scopus 로고    scopus 로고
    • Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions
    • Ballinger C.A., Connell P., Wu Y., Hu Z., Thompson L.J., Yin L.Y., et al. Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. Mol Cell Biol 1999, 19(6):4535-4545.
    • (1999) Mol Cell Biol , vol.19 , Issue.6 , pp. 4535-4545
    • Ballinger, C.A.1    Connell, P.2    Wu, Y.3    Hu, Z.4    Thompson, L.J.5    Yin, L.Y.6
  • 72
    • 0035146685 scopus 로고    scopus 로고
    • The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins
    • Connell P., Ballinger C.A., Jiang J., Wu Y., Thompson L.J., Hohfeld J., et al. The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins. Nat Cell Biol 2001, 3(1):93-96.
    • (2001) Nat Cell Biol , vol.3 , Issue.1 , pp. 93-96
    • Connell, P.1    Ballinger, C.A.2    Jiang, J.3    Wu, Y.4    Thompson, L.J.5    Hohfeld, J.6
  • 73
    • 0035684430 scopus 로고    scopus 로고
    • CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein
    • Murata S., Minami Y., Minami M., Chiba T., Tanaka K. CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein. EMBO Rep 2001, 2(12):1133-1138.
    • (2001) EMBO Rep , vol.2 , Issue.12 , pp. 1133-1138
    • Murata, S.1    Minami, Y.2    Minami, M.3    Chiba, T.4    Tanaka, K.5
  • 74
    • 77955257617 scopus 로고    scopus 로고
    • CHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70-bound substrates
    • Stankiewicz M., Nikolay R., Rybin V., Mayer M.P. CHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70-bound substrates. FEBS J 2010, 277(16):3353-3367.
    • (2010) FEBS J , vol.277 , Issue.16 , pp. 3353-3367
    • Stankiewicz, M.1    Nikolay, R.2    Rybin, V.3    Mayer, M.P.4
  • 76
    • 0033534588 scopus 로고    scopus 로고
    • An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators
    • Takayama S., Xie Z., Reed J.C. An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators. J Biol Chem 1999, 274(2):781-786.
    • (1999) J Biol Chem , vol.274 , Issue.2 , pp. 781-786
    • Takayama, S.1    Xie, Z.2    Reed, J.C.3
  • 77
    • 33644690646 scopus 로고    scopus 로고
    • Regulation of the cytoplasmic quality control protein degradation pathway by BAG2
    • Dai Q., Qian S.B., Li H.H., McDonough H., Borchers C., Huang D., et al. Regulation of the cytoplasmic quality control protein degradation pathway by BAG2. J Biol Chem 2005, 280(46):38673-38681.
    • (2005) J Biol Chem , vol.280 , Issue.46 , pp. 38673-38681
    • Dai, Q.1    Qian, S.B.2    Li, H.H.3    McDonough, H.4    Borchers, C.5    Huang, D.6
  • 78
    • 79951925183 scopus 로고    scopus 로고
    • Ubiquitinylation of alpha-synuclein by carboxyl terminus Hsp70-interacting protein (CHIP) is regulated by Bcl-2-associated athanogene 5 (BAG5)
    • Kalia L.V., Kalia S.K., Chau H., Lozano A.M., Hyman B.T., McLean P.J. Ubiquitinylation of alpha-synuclein by carboxyl terminus Hsp70-interacting protein (CHIP) is regulated by Bcl-2-associated athanogene 5 (BAG5). PLoS One 2011, 6(2):e14695.
    • (2011) PLoS One , vol.6 , Issue.2
    • Kalia, L.V.1    Kalia, S.K.2    Chau, H.3    Lozano, A.M.4    Hyman, B.T.5    McLean, P.J.6
  • 79
    • 0039172708 scopus 로고    scopus 로고
    • The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome
    • Luders J., Demand J., Hohfeld J. The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome. J Biol Chem 2000, 275(7):4613-4617.
    • (2000) J Biol Chem , vol.275 , Issue.7 , pp. 4613-4617
    • Luders, J.1    Demand, J.2    Hohfeld, J.3
  • 80
    • 65449117176 scopus 로고    scopus 로고
    • Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3
    • Gamerdinger M., Hajieva P., Kaya A.M., Wolfrum U., Hartl F.U., Behl C. Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3. EMBO J 2009, 28(7):889-901.
    • (2009) EMBO J , vol.28 , Issue.7 , pp. 889-901
    • Gamerdinger, M.1    Hajieva, P.2    Kaya, A.M.3    Wolfrum, U.4    Hartl, F.U.5    Behl, C.6
  • 81
    • 4344578534 scopus 로고    scopus 로고
    • The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator
    • Alberti S., Bohse K., Arndt V., Schmitz A., Hohfeld J. The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator. Mol Biol Cell 2004, 15(9):4003-4010.
    • (2004) Mol Biol Cell , vol.15 , Issue.9 , pp. 4003-4010
    • Alberti, S.1    Bohse, K.2    Arndt, V.3    Schmitz, A.4    Hohfeld, J.5
  • 82
    • 77954178073 scopus 로고    scopus 로고
    • A nucleus-based quality control mechanism for cytosolic proteins
    • Prasad R., Kawaguchi S., Ng D.T. A nucleus-based quality control mechanism for cytosolic proteins. Mol Biol Cell 2010, 21(13):2117-2127.
    • (2010) Mol Biol Cell , vol.21 , Issue.13 , pp. 2117-2127
    • Prasad, R.1    Kawaguchi, S.2    Ng, D.T.3
  • 83
    • 77954196466 scopus 로고    scopus 로고
    • Ubr1 and Ubr2 function in a quality control pathway for degradation of unfolded cytosolic proteins
    • Nillegoda N.B., Theodoraki M.A., Mandal A.K., Mayo K.J., Ren H.Y., Sultana R., et al. Ubr1 and Ubr2 function in a quality control pathway for degradation of unfolded cytosolic proteins. Mol Biol Cell 2010, 21(13):2102-2116.
    • (2010) Mol Biol Cell , vol.21 , Issue.13 , pp. 2102-2116
    • Nillegoda, N.B.1    Theodoraki, M.A.2    Mandal, A.K.3    Mayo, K.J.4    Ren, H.Y.5    Sultana, R.6
  • 84
    • 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 2010, 107(3):1106-1111.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.3 , pp. 1106-1111
    • Heck, J.W.1    Cheung, S.K.2    Hampton, R.Y.3
  • 85
    • 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 2008, 582(30):4143-4146.
    • (2008) FEBS Lett , vol.582 , Issue.30 , pp. 4143-4146
    • Eisele, F.1    Wolf, D.H.2
  • 86
    • 79960683356 scopus 로고    scopus 로고
    • The N-end rule pathway and regulation by proteolysis
    • Varshavsky A. The N-end rule pathway and regulation by proteolysis. Protein Sci 2011, 20(8):1298-1345.
    • (2011) Protein Sci , vol.20 , Issue.8 , pp. 1298-1345
    • Varshavsky, A.1
  • 87
    • 81355127301 scopus 로고    scopus 로고
    • UBR1 promotes protein kinase quality control and sensitizes cells to Hsp90 inhibition
    • Sultana R., Theodoraki M.A., Caplan A.J. UBR1 promotes protein kinase quality control and sensitizes cells to Hsp90 inhibition. Exp Cell Res 2011, 318(1):53-60.
    • (2011) Exp Cell Res , vol.318 , Issue.1 , pp. 53-60
    • Sultana, R.1    Theodoraki, M.A.2    Caplan, A.J.3
  • 88
    • 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., Bolender N., Eisele F., Kostova Z., Takeuchi J., Coffino P., 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 2007, 18(1):153-165.
    • (2007) Mol Biol Cell , vol.18 , Issue.1 , pp. 153-165
    • Park, S.H.1    Bolender, N.2    Eisele, F.3    Kostova, Z.4    Takeuchi, J.5    Coffino, P.6
  • 89
    • 77149120798 scopus 로고    scopus 로고
    • N-terminal acetylation of cellular proteins creates specific degradation signals
    • Hwang C.S., Shemorry A., Varshavsky A. N-terminal acetylation of cellular proteins creates specific degradation signals. Science 2010, 327(5968):973-977.
    • (2010) Science , vol.327 , Issue.5968 , pp. 973-977
    • Hwang, C.S.1    Shemorry, A.2    Varshavsky, A.3
  • 90
    • 80455122748 scopus 로고    scopus 로고
    • Hul5 HECT ubiquitin ligase plays a major role in the ubiquitylation and turnover of cytosolic misfolded proteins
    • Fang N.N., Ng A.H., Measday V., Mayor T. Hul5 HECT ubiquitin ligase plays a major role in the ubiquitylation and turnover of cytosolic misfolded proteins. Nat Cell Biol 2011, 13(11):1344-1352.
    • (2011) Nat Cell Biol , vol.13 , Issue.11 , pp. 1344-1352
    • Fang, N.N.1    Ng, A.H.2    Measday, V.3    Mayor, T.4
  • 91
    • 0036753063 scopus 로고    scopus 로고
    • Multiple associated proteins regulate proteasome structure and function
    • Leggett D.S., Hanna J., Borodovsky A., Crosas B., Schmidt M., Baker R.T., et al. Multiple associated proteins regulate proteasome structure and function. Mol Cell 2002, 10(3):495-507.
    • (2002) Mol Cell , vol.10 , Issue.3 , pp. 495-507
    • Leggett, D.S.1    Hanna, J.2    Borodovsky, A.3    Crosas, B.4    Schmidt, M.5    Baker, R.T.6
  • 92
    • 75749101797 scopus 로고    scopus 로고
    • The ubiquitin ligase Hul5 promotes proteasomal processivity
    • Aviram S., Kornitzer D. The ubiquitin ligase Hul5 promotes proteasomal processivity. Mol Cell Biol 2010, 30(4):985-994.
    • (2010) Mol Cell Biol , vol.30 , Issue.4 , pp. 985-994
    • Aviram, S.1    Kornitzer, D.2
  • 93
    • 38849113244 scopus 로고    scopus 로고
    • Messenger RNA surveillance systems monitoring proper translation termination
    • Akimitsu N. Messenger RNA surveillance systems monitoring proper translation termination. J Biochem 2008, 143(1):1-8.
    • (2008) J Biochem , vol.143 , Issue.1 , pp. 1-8
    • Akimitsu, N.1
  • 94
    • 66849136862 scopus 로고    scopus 로고
    • Nascent peptide-dependent translation arrest leads to Not4p-mediated protein degradation by the proteasome
    • Dimitrova L.N., Kuroha K., Tatematsu T., Inada T. Nascent peptide-dependent translation arrest leads to Not4p-mediated protein degradation by the proteasome. J Biol Chem 2009, 284(16):10343-10352.
    • (2009) J Biol Chem , vol.284 , Issue.16 , pp. 10343-10352
    • Dimitrova, L.N.1    Kuroha, K.2    Tatematsu, T.3    Inada, T.4
  • 95
    • 35548981256 scopus 로고    scopus 로고
    • A genomic screen in yeast reveals novel aspects of nonstop mRNA metabolism
    • Wilson M.A., Meaux S., van Hoof A. A genomic screen in yeast reveals novel aspects of nonstop mRNA metabolism. Genetics 2007, 177(2):773-784.
    • (2007) Genetics , vol.177 , Issue.2 , pp. 773-784
    • Wilson, M.A.1    Meaux, S.2    van Hoof, A.3
  • 96
    • 34147207885 scopus 로고    scopus 로고
    • Identification of Rkr1, a nuclear RING domain protein with functional connections to chromatin modification in Saccharomyces cerevisiae
    • Braun M.A., Costa P.J., Crisucci E.M., Arndt K.M. Identification of Rkr1, a nuclear RING domain protein with functional connections to chromatin modification in Saccharomyces cerevisiae. Mol Cell Biol 2007, 27(8):2800-2811.
    • (2007) Mol Cell Biol , vol.27 , Issue.8 , pp. 2800-2811
    • Braun, M.A.1    Costa, P.J.2    Crisucci, E.M.3    Arndt, K.M.4
  • 97
    • 77957169824 scopus 로고    scopus 로고
    • Role of a ribosome-associated E3 ubiquitin ligase in protein quality control
    • Bengtson M.H., Joazeiro C.A. Role of a ribosome-associated E3 ubiquitin ligase in protein quality control. Nature 2010, 467(7314):470-473.
    • (2010) Nature , vol.467 , Issue.7314 , pp. 470-473
    • Bengtson, M.H.1    Joazeiro, C.A.2
  • 98
    • 3042618914 scopus 로고    scopus 로고
    • Sir antagonist 1 (San1) is a ubiquitin ligase
    • Dasgupta A., Ramsey K.L., Smith J.S., Auble D.T. Sir antagonist 1 (San1) is a ubiquitin ligase. J Biol Chem 2004, 279(26):26830-26838.
    • (2004) J Biol Chem , vol.279 , Issue.26 , pp. 26830-26838
    • Dasgupta, A.1    Ramsey, K.L.2    Smith, J.S.3    Auble, D.T.4
  • 99
    • 17644396667 scopus 로고    scopus 로고
    • Degradation-mediated protein quality control in the nucleus
    • Gardner R.G., Nelson Z.W., Gottschling D.E. Degradation-mediated protein quality control in the nucleus. Cell 2005, 120(6):803-815.
    • (2005) Cell , vol.120 , Issue.6 , pp. 803-815
    • Gardner, R.G.1    Nelson, Z.W.2    Gottschling, D.E.3
  • 100
    • 0031760928 scopus 로고    scopus 로고
    • The yeast protein complex containing cdc68 and pob3 mediates core-promoter repression through the cdc68 N-terminal domain
    • Evans D.R., Brewster N.K., Xu Q., Rowley A., Altheim B.A., Johnston G.C., et al. The yeast protein complex containing cdc68 and pob3 mediates core-promoter repression through the cdc68 N-terminal domain. Genetics 1998, 150(4):1393-1405.
    • (1998) Genetics , vol.150 , Issue.4 , pp. 1393-1405
    • Evans, D.R.1    Brewster, N.K.2    Xu, Q.3    Rowley, A.4    Altheim, B.A.5    Johnston, G.C.6
  • 101
    • 57649232249 scopus 로고    scopus 로고
    • A genetic screen in Saccharomyces cerevisiae identifies new genes that interact with mex67-5, a temperature-sensitive allele of the gene encoding the mRNA export receptor
    • Estruch F., Peiro-Chova L., Gomez-Navarro N., Durban J., Hodge C., Del Olmo M., et al. A genetic screen in Saccharomyces cerevisiae identifies new genes that interact with mex67-5, a temperature-sensitive allele of the gene encoding the mRNA export receptor. Mol Genet Genomics 2009, 281(1):125-134.
    • (2009) Mol Genet Genomics , vol.281 , Issue.1 , pp. 125-134
    • Estruch, F.1    Peiro-Chova, L.2    Gomez-Navarro, N.3    Durban, J.4    Hodge, C.5    Del Olmo, M.6
  • 102
    • 64249163620 scopus 로고    scopus 로고
    • Inefficient quality control of thermosensitive proteins on the plasma membrane
    • Lewis M.J., Pelham H.R. Inefficient quality control of thermosensitive proteins on the plasma membrane. PLoS One 2009, 4(4):e5038.
    • (2009) PLoS One , vol.4 , Issue.4
    • Lewis, M.J.1    Pelham, H.R.2
  • 103
    • 79953907268 scopus 로고    scopus 로고
    • Nuclear protein quality is regulated by the ubiquitin-proteasome system through the activity of Ubc4 and San1 in fission yeast
    • Matsuo Y., Kishimoto H., Tanae K., Kitamura K., Katayama S., Kawamukai M. Nuclear protein quality is regulated by the ubiquitin-proteasome system through the activity of Ubc4 and San1 in fission yeast. J Biol Chem 2011.
    • (2011) J Biol Chem
    • Matsuo, Y.1    Kishimoto, H.2    Tanae, K.3    Kitamura, K.4    Katayama, S.5    Kawamukai, M.6
  • 104
    • 78650731442 scopus 로고    scopus 로고
    • Disorder targets misorder in nuclear quality control degradation: a disordered ubiquitin ligase directly recognizes its misfolded substrates
    • Rosenbaum J.C., Fredrickson E.K., Oeser M.L., Garrett-Engele C.M., Locke M.N., Richardson L.A., et al. Disorder targets misorder in nuclear quality control degradation: a disordered ubiquitin ligase directly recognizes its misfolded substrates. Mol Cell 2011, 41(1):93-106.
    • (2011) Mol Cell , vol.41 , Issue.1 , pp. 93-106
    • Rosenbaum, J.C.1    Fredrickson, E.K.2    Oeser, M.L.3    Garrett-Engele, C.M.4    Locke, M.N.5    Richardson, L.A.6
  • 105
    • 79959888485 scopus 로고    scopus 로고
    • Exposed hydrophobicity is a key determinant of nuclear quality control degradation
    • Fredrickson E.K., Rosenbaum J.C., Locke M.N., Milac T.I., Gardner R.G. Exposed hydrophobicity is a key determinant of nuclear quality control degradation. Mol Biol Cell 2011, 22(13):2384-2395.
    • (2011) Mol Biol Cell , vol.22 , Issue.13 , pp. 2384-2395
    • Fredrickson, E.K.1    Rosenbaum, J.C.2    Locke, M.N.3    Milac, T.I.4    Gardner, R.G.5
  • 106
    • 33750349837 scopus 로고    scopus 로고
    • Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase
    • Deng M., Hochstrasser M. Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase. Nature 2006, 443(7113):827-831.
    • (2006) Nature , vol.443 , Issue.7113 , pp. 827-831
    • Deng, M.1    Hochstrasser, M.2
  • 107
    • 84055200360 scopus 로고    scopus 로고
    • Exposure of bipartite hydrophobic signal triggers nuclear quality control of Ndc10 at the endoplasmic reticulum/nuclear envelope
    • Furth N., Gertman O., Shiber A., Alfassy O.S., Cohen I., Rosenberg M., et al. Exposure of bipartite hydrophobic signal triggers nuclear quality control of Ndc10 at the endoplasmic reticulum/nuclear envelope. Mol Biol Cell 2011.
    • (2011) Mol Biol Cell
    • Furth, N.1    Gertman, O.2    Shiber, A.3    Alfassy, O.S.4    Cohen, I.5    Rosenberg, M.6
  • 108
    • 50649104647 scopus 로고    scopus 로고
    • Activation of the Slx5-Slx8 ubiquitin ligase by poly-small ubiquitin-like modifier conjugates
    • Mullen J.R., Brill S.J. Activation of the Slx5-Slx8 ubiquitin ligase by poly-small ubiquitin-like modifier conjugates. J Biol Chem 2008, 283(29):19912-19921.
    • (2008) J Biol Chem , vol.283 , Issue.29 , pp. 19912-19921
    • Mullen, J.R.1    Brill, S.J.2
  • 109
    • 36348964395 scopus 로고    scopus 로고
    • The yeast Hex3.Slx8 heterodimer is a ubiquitin ligase stimulated by substrate sumoylation
    • Xie Y., Kerscher O., Kroetz M.B., McConchie H.F., Sung P., Hochstrasser M. The yeast Hex3.Slx8 heterodimer is a ubiquitin ligase stimulated by substrate sumoylation. J Biol Chem 2007, 282(47):34176-34184.
    • (2007) J Biol Chem , vol.282 , Issue.47 , pp. 34176-34184
    • Xie, Y.1    Kerscher, O.2    Kroetz, M.B.3    McConchie, H.F.4    Sung, P.5    Hochstrasser, M.6
  • 110
    • 63049110916 scopus 로고    scopus 로고
    • Quality control of a transcriptional regulator by SUMO-targeted degradation
    • Wang Z., Prelich G. Quality control of a transcriptional regulator by SUMO-targeted degradation. Mol Cell Biol 2009, 29(7):1694-1706.
    • (2009) Mol Cell Biol , vol.29 , Issue.7 , pp. 1694-1706
    • Wang, Z.1    Prelich, G.2
  • 111
    • 0028006681 scopus 로고
    • Intracellular turnover of cystic fibrosis transmembrane conductance regulator. Inefficient processing and rapid degradation of wild-type and mutant proteins
    • Ward C.L., Kopito R.R. Intracellular turnover of cystic fibrosis transmembrane conductance regulator. Inefficient processing and rapid degradation of wild-type and mutant proteins. J Biol Chem 1994, 269(41):25710-25718.
    • (1994) J Biol Chem , vol.269 , Issue.41 , pp. 25710-25718
    • Ward, C.L.1    Kopito, R.R.2
  • 112
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward C.L., Omura S., Kopito R.R. Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 1995, 83(1):121-127.
    • (1995) Cell , vol.83 , Issue.1 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 113
    • 65649121163 scopus 로고    scopus 로고
    • Intra-nuclear degradation of polyglutamine aggregates by the ubiquitin proteasome system
    • Iwata A., Nagashima Y., Matsumoto L., Suzuki T., Yamanaka T., Date H., et al. Intra-nuclear degradation of polyglutamine aggregates by the ubiquitin proteasome system. J Biol Chem 2009, 284(15):9796-9803.
    • (2009) J Biol Chem , vol.284 , Issue.15 , pp. 9796-9803
    • Iwata, A.1    Nagashima, Y.2    Matsumoto, L.3    Suzuki, T.4    Yamanaka, T.5    Date, H.6
  • 114
    • 33745612063 scopus 로고    scopus 로고
    • PML clastosomes prevent nuclear accumulation of mutant ataxin-7 and other polyglutamine proteins
    • Janer A., Martin E., Muriel M.P., Latouche M., Fujigasaki H., Ruberg M., et al. PML clastosomes prevent nuclear accumulation of mutant ataxin-7 and other polyglutamine proteins. J Cell Biol 2006, 174(1):65-76.
    • (2006) J Cell Biol , vol.174 , Issue.1 , pp. 65-76
    • Janer, A.1    Martin, E.2    Muriel, M.P.3    Latouche, M.4    Fujigasaki, H.5    Ruberg, M.6
  • 115
    • 26244451787 scopus 로고    scopus 로고
    • Nuclear aggresomes form by fusion of PML-associated aggregates
    • Fu L., Gao Y.S., Tousson A., Shah A., Chen T.L., Vertel B.M., et al. Nuclear aggresomes form by fusion of PML-associated aggregates. Mol Biol Cell 2005, 16(10):4905-4917.
    • (2005) Mol Biol Cell , vol.16 , Issue.10 , pp. 4905-4917
    • Fu, L.1    Gao, Y.S.2    Tousson, A.3    Shah, A.4    Chen, T.L.5    Vertel, B.M.6
  • 116
    • 0034505937 scopus 로고    scopus 로고
    • Protein degradation in mitochondria
    • Kaser M., Langer T. Protein degradation in mitochondria. Semin Cell Dev Biol 2000, 11(3):181-190.
    • (2000) Semin Cell Dev Biol , vol.11 , Issue.3 , pp. 181-190
    • Kaser, M.1    Langer, T.2
  • 117
    • 0032499264 scopus 로고    scopus 로고
    • Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
    • Kitada T., Asakawa S., Hattori N., Matsumine H., Yamamura Y., Minoshima S., et al. Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature 1998, 392(6676):605-608.
    • (1998) Nature , vol.392 , Issue.6676 , pp. 605-608
    • Kitada, T.1    Asakawa, S.2    Hattori, N.3    Matsumine, H.4    Yamamura, Y.5    Minoshima, S.6
  • 118
    • 0033151716 scopus 로고    scopus 로고
    • A novel transactivation domain in parkin
    • Morett E., Bork P. A novel transactivation domain in parkin. Trends Biochem Sci 1999, 24(6):229-231.
    • (1999) Trends Biochem Sci , vol.24 , Issue.6 , pp. 229-231
    • Morett, E.1    Bork, P.2
  • 119
    • 0033933048 scopus 로고    scopus 로고
    • Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase
    • Shimura H., Hattori N., Kubo S., Mizuno Y., Asakawa S., Minoshima S., et al. Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase. Nat Genet 2000, 25(3):302-305.
    • (2000) Nat Genet , vol.25 , Issue.3 , pp. 302-305
    • Shimura, H.1    Hattori, N.2    Kubo, S.3    Mizuno, Y.4    Asakawa, S.5    Minoshima, S.6
  • 120
    • 0034700158 scopus 로고    scopus 로고
    • Parkin functions as an E2-dependent ubiquitin-protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1
    • Zhang Y., Gao J., Chung K.K., Huang H., Dawson V.L., Dawson T.M. Parkin functions as an E2-dependent ubiquitin-protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1. Proc Natl Acad Sci USA 2000, 97(24):13354-13359.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.24 , pp. 13354-13359
    • Zhang, Y.1    Gao, J.2    Chung, K.K.3    Huang, H.4    Dawson, V.L.5    Dawson, T.M.6
  • 121
    • 0036345454 scopus 로고    scopus 로고
    • CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity
    • Imai Y., Soda M., Hatakeyama S., Akagi T., Hashikawa T., Nakayama K.I., et al. CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity. Mol Cell 2002, 10(1):55-67.
    • (2002) Mol Cell , vol.10 , Issue.1 , pp. 55-67
    • Imai, Y.1    Soda, M.2    Hatakeyama, S.3    Akagi, T.4    Hashikawa, T.5    Nakayama, K.I.6
  • 123
    • 33747613595 scopus 로고    scopus 로고
    • A novel mitochondrial ubiquitin ligase plays a critical role in mitochondrial dynamics
    • Yonashiro R., Ishido S., Kyo S., Fukuda T., Goto E., Matsuki Y., et al. A novel mitochondrial ubiquitin ligase plays a critical role in mitochondrial dynamics. EMBO J 2006, 25(15):3618-3626.
    • (2006) EMBO J , vol.25 , Issue.15 , pp. 3618-3626
    • Yonashiro, R.1    Ishido, S.2    Kyo, S.3    Fukuda, T.4    Goto, E.5    Matsuki, Y.6
  • 124
    • 73949112709 scopus 로고    scopus 로고
    • Mitochondrial ubiquitin ligase MITOL ubiquitinates mutant SOD1 and attenuates mutant SOD1-induced reactive oxygen species generation
    • Yonashiro R., Sugiura A., Miyachi M., Fukuda T., Matsushita N., Inatome R., et al. Mitochondrial ubiquitin ligase MITOL ubiquitinates mutant SOD1 and attenuates mutant SOD1-induced reactive oxygen species generation. Mol Biol Cell 2009, 20(21):4524-4530.
    • (2009) Mol Biol Cell , vol.20 , Issue.21 , pp. 4524-4530
    • Yonashiro, R.1    Sugiura, A.2    Miyachi, M.3    Fukuda, T.4    Matsushita, N.5    Inatome, R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.