메뉴 건너뛰기




Volumn 13, Issue 5, 2012, Pages 436-446

Roles of p97-associated deubiquitinases in protein quality control at the endoplasmic reticulum

Author keywords

Ataxin 3; Deubiquitination; ER protein quality control; ERAD retrotranslocation; p97 VCP Cdc48; Proteasome; Ubiquitin; YOD1

Indexed keywords

ATAXIN 3; LIGASE; PROTEIN P97; PROTEIN P97 ASSOCIATED DEUBIQUITINASE; UBIQUITIN; UNCLASSIFIED DRUG; YOD1;

EID: 84866527405     PISSN: 13892037     EISSN: 18755550     Source Type: Journal    
DOI: 10.2174/138920312802430608     Document Type: Article
Times cited : (44)

References (99)
  • 1
    • 0036270698 scopus 로고    scopus 로고
    • Retro-translocation of proteins from the endoplasmic reticulum into the cytosol
    • Tsai, B.; Ye, Y.; Rapoport, T. A. Retro-translocation of proteins from the endoplasmic reticulum into the cytosol. Nat. Rev. Mol. Cell Biol., 2002, 3, 246-255.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 246-255
    • Tsai, B.1    Ye, Y.2    Rapoport, T.A.3
  • 2
    • 56749176947 scopus 로고    scopus 로고
    • One step at a time: Endoplasmic reticulum-associated degradation
    • Vembar, S. S.; Brodsky, J. L. One step at a time: endoplasmic reticulum-associated degradation. Nat. Rev. Mol. Cell Biol., 2008, 9, 944-957.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 944-957
    • Vembar, S.S.1    Brodsky, J.L.2
  • 3
    • 79960066445 scopus 로고    scopus 로고
    • Proteostasis regulation at the endoplasmic reticulum: A new perturbation site for targeted cancer therapy
    • Liu, Y.; Ye, Y. Proteostasis regulation at the endoplasmic reticulum: a new perturbation site for targeted cancer therapy. Cell Res., 2011, 21, 867-883.
    • (2011) Cell Res. , vol.21 , pp. 867-883
    • Liu, Y.1    Ye, Y.2
  • 4
    • 27144478935 scopus 로고    scopus 로고
    • The role of the ubiquitin-proteasome system in ER quality control
    • Ye, Y. The role of the ubiquitin-proteasome system in ER quality control. Essays Biochem., 2005, 41, 99-112.
    • (2005) Essays Biochem. , vol.41 , pp. 99-112
    • Ye, Y.1
  • 5
    • 63649161943 scopus 로고    scopus 로고
    • The ubiquitylation machinery of the endoplasmic reticulum
    • Hirsch, C.; Gauss, R.; Horn, S. C.; Neuber, O.; Sommer, T. The ubiquitylation machinery of the endoplasmic reticulum. Nature, 2009, 458, 453-460.
    • (2009) Nature , vol.458 , pp. 453-460
    • Hirsch, C.1    Gauss, R.2    Horn, S.C.3    Neuber, O.4    Sommer, T.5
  • 6
    • 0038487228 scopus 로고    scopus 로고
    • Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: Dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains
    • Ye, Y.; Meyer, H. H.; Rapoport, T. A. Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains. J. Cell Biol., 2003, 162, 71-84.
    • (2003) J. Cell Biol. , vol.162 , pp. 71-84
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 7
    • 0041315902 scopus 로고    scopus 로고
    • Polyubiquitin serves as a recognition signal, rather than a ratcheting molecule, during retrotranslocation of proteins across the endoplasmic reticulum membrane
    • Flierman, D.; Ye, Y.; Dai, M.; Chau, V.; Rapoport, T. A. Polyubiquitin serves as a recognition signal, rather than a ratcheting molecule, during retrotranslocation of proteins across the endoplasmic reticulum membrane. J. Biol. Chem., 2003, 278, 34774-34782.
    • (2003) J. Biol. Chem. , vol.278 , pp. 34774-34782
    • Flierman, D.1    Ye, Y.2    Dai, M.3    Chau, V.4    Rapoport, T.A.5
  • 8
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • Sowa, M. E.; Bennett, E. J.; Gygi, S. P.; Harper, J. W. Defining the human deubiquitinating enzyme interaction landscape. Cell, 2009, 138, 389-403.
    • (2009) Cell , vol.138 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.W.4
  • 9
    • 79955470830 scopus 로고    scopus 로고
    • Trimming of ubiquitin chains by proteasome-associated deubiquitinating enzymes
    • Lee, M. J.; Lee, B. H.; Hanna, J.; King, R. W.; Finley, D. Trimming of ubiquitin chains by proteasome-associated deubiquitinating enzymes. Mol. Cell Proteomics, 2011, 10, R110 003871.
    • (2011) Mol. Cell Proteomics , vol.10
    • Lee, M.J.1    Lee, B.H.2    Hanna, J.3    King, R.W.4    Finley, D.5
  • 10
    • 67650620318 scopus 로고    scopus 로고
    • Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes
    • Reyes-Turcu, F. E.; Ventii, K. H.; Wilkinson, K. D. Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes. Annu. Rev. Biochem., 2009, 78, 363-397.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 363-397
    • Reyes-Turcu, F.E.1    Ventii, K.H.2    Wilkinson, K.D.3
  • 11
    • 0027327659 scopus 로고
    • A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum
    • Sommer, T.; Jentsch, S. A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum. Nature, 1993, 365, 176-179.
    • (1993) Nature , vol.365 , pp. 176-179
    • Sommer, T.1    Jentsch, S.2
  • 12
    • 0029838640 scopus 로고    scopus 로고
    • ER degradation of a misfolded luminal protein by the cytosolic ubiquitinproteasome pathway
    • Hiller, M. M.; Finger, A.; Schweiger, M.; Wolf, D. H. ER degradation of a misfolded luminal protein by the cytosolic ubiquitinproteasome pathway. Science, 1996, 273, 1725-1728.
    • (1996) Science , vol.273 , pp. 1725-1728
    • Hiller, M.M.1    Finger, A.2    Schweiger, M.3    Wolf, D.H.4
  • 13
    • 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, 379-384.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 379-384
    • Friedlander, R.1    Jarosch, E.2    Urban, J.3    Volkwein, C.4    Sommer, T.5
  • 14
    • 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, 24-29.
    • (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
  • 15
    • 70350461507 scopus 로고    scopus 로고
    • Building ubiquitin chains: E2 enzymes at work
    • Ye, Y.; Rape, M. Building ubiquitin chains: E2 enzymes at work. Nat. Rev. Mol. Cell Biol., 2009, 10, 755-764.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 755-764
    • Ye, Y.1    Rape, M.2
  • 16
    • 0035844139 scopus 로고    scopus 로고
    • Endoplasmic reticulum (ER)-associated degradation of T cell receptor subunits. Involvement of ER-associated ubiquitin-conjugating enzymes (E2s)
    • Tiwari, S.; Weissman, A. M. Endoplasmic reticulum (ER)-associated degradation of T cell receptor subunits. Involvement of ER-associated ubiquitin-conjugating enzymes (E2s). J. Biol. Chem., 2001, 276, 16193-16200.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16193-16200
    • Tiwari, S.1    Weissman, A.M.2
  • 18
    • 31044437051 scopus 로고    scopus 로고
    • The activity of a human endoplasmic reticulumassociated 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 reticulumassociated degradation E3, gp78, requires its Cue domain, RING finger, and an E2-binding site. Proc. Natl. Acad. Sci. USA, 2006, 103, 341-346.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 341-346
    • Chen, B.1    Mariano, J.2    Tsai, Y.C.3    Chan, A.H.4    Cohen, M.5    Weissman, A.M.6
  • 20
    • 74049086778 scopus 로고    scopus 로고
    • Ube2j2 ubiquitinates hydroxylated amino acids on ER-associated degradation substrates
    • Wang, X.; Herr, R. A.; Rabelink, M.; Hoeben, R. C.; Wiertz, E. J.; Hansen, T. H. Ube2j2 ubiquitinates hydroxylated amino acids on ER-associated degradation substrates. J. Cell Biol., 2009, 187, 655-668.
    • (2009) J. Cell Biol. , vol.187 , pp. 655-668
    • Wang, X.1    Herr, R.A.2    Rabelink, M.3    Hoeben, R.C.4    Wiertz, E.J.5    Hansen, T.H.6
  • 21
    • 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, 10663-10669.
    • (2001) J. Biol. Chem. , vol.276 , pp. 10663-10669
    • Deak, P.M.1    Wolf, D.H.2
  • 22
    • 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, 2660-2674.
    • (2001) Genes Dev. , vol.15 , pp. 2660-2674
    • Swanson, R.1    Locher, M.2    Hochstrasser, M.3
  • 24
    • 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, 14422-14427.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14422-14427
    • Fang, S.1    Ferrone, M.2    Yang, C.3    Jensen, J.P.4    Tiwari, S.5    Weissman, A.M.6
  • 25
    • 33748792529 scopus 로고    scopus 로고
    • Ubiquitin ligase gp78 increases solubility and facilitates degradation of the Z variant of alpha-1-antitrypsin
    • Shen, Y.; Ballar, P.; Fang, S. Ubiquitin ligase gp78 increases solubility and facilitates degradation of the Z variant of alpha-1-antitrypsin. Biochem. Biophys. Res. Commun., 2006, 349, 1285-1293.
    • (2006) Biochem. Biophys. Res. Commun. , vol.349 , pp. 1285-1293
    • Shen, Y.1    Ballar, P.2    Fang, S.3
  • 26
    • 24944591120 scopus 로고    scopus 로고
    • Gp78, a membraneanchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase
    • Song, B. L.; Sever, N.; DeBose-Boyd, R. A. Gp78, a membraneanchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase. Mol. Cell, 2005, 19, 829-840.
    • (2005) Mol. Cell , vol.19 , pp. 829-840
    • Song, B.L.1    Sever, N.2    DeBose-Boyd, R.A.3
  • 28
    • 33746675669 scopus 로고    scopus 로고
    • Sequential quality-control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator
    • Younger, J. M.; Chen, L.; Ren, H. Y.; Rosser, M. F.; Turnbull, E. L.; Fan, C. Y.; Patterson, C.; Cyr, D. M. Sequential quality-control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator. Cell, 2006, 126, 571-582.
    • (2006) Cell , vol.126 , pp. 571-582
    • Younger, J.M.1    Chen, L.2    Ren, H.Y.3    Rosser, M.F.4    Turnbull, E.L.5    Fan, C.Y.6    Patterson, C.7    Cyr, D.M.8
  • 29
    • 77952929246 scopus 로고    scopus 로고
    • RNF-121 is an endoplasmic reticulum-membrane E3 ubiquitin ligase involved in the regulation of beta-integrin
    • Darom, A.; Bening-Abu-Shach, U.; Broday, L. RNF-121 is an endoplasmic reticulum-membrane E3 ubiquitin ligase involved in the regulation of beta-integrin. Mol. Biol. Cell, 2011, 21, 1788-1798.
    • (2011) Mol. Biol. Cell , vol.21 , pp. 1788-1798
    • Darom, A.1    Bening-Abu-Shach, U.2    Broday, L.3
  • 30
    • 79959888488 scopus 로고    scopus 로고
    • RNF170 protein, an endoplasmic reticulum membrane ubiquitin ligase, mediates inositol 1,4,5-trisphosphate receptor ubiquitination and degradation
    • Lu, J. P.; Wang, Y.; Sliter, D. A.; Pearce, M. M.; Wojcikiewicz, R. J. RNF170 protein, an endoplasmic reticulum membrane ubiquitin ligase, mediates inositol 1,4,5-trisphosphate receptor ubiquitination and degradation. J. Biol. Chem., 2011, 286, 24426-24433.
    • (2011) J. Biol. Chem. , vol.286 , pp. 24426-24433
    • Lu, J.P.1    Wang, Y.2    Sliter, D.A.3    Pearce, M.M.4    Wojcikiewicz, R.J.5
  • 31
    • 0035142877 scopus 로고    scopus 로고
    • The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
    • Meacham, G. C.; Patterson, C.; Zhang, W.; Younger, J. M.; Cyr, D. M. The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nat. Cell Biol., 2001, 3, 100-105.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 100-105
    • Meacham, G.C.1    Patterson, C.2    Zhang, W.3    Younger, J.M.4    Cyr, D.M.5
  • 32
    • 0035967883 scopus 로고    scopus 로고
    • An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin
    • Imai, Y.; Soda, M.; Inoue, H.; Hattori, N.; Mizuno, Y.; Takahashi, R. An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin. Cell, 2001, 105, 891-902.
    • (2001) Cell , vol.105 , pp. 891-902
    • Imai, Y.1    Soda, M.2    Inoue, H.3    Hattori, N.4    Mizuno, Y.5    Takahashi, R.6
  • 34
    • 0242321836 scopus 로고    scopus 로고
    • Fbs2 is a new member of the E3 ubiquitin ligase family that recognizes sugar chains
    • Yoshida, Y.; Tokunaga, F.; Chiba, T.; Iwai, K.; Tanaka, K.; Tai, T. Fbs2 is a new member of the E3 ubiquitin ligase family that recognizes sugar chains. J. Biol. Chem., 2003, 278, 43877-43884.
    • (2003) J. Biol. Chem. , vol.278 , pp. 43877-43884
    • Yoshida, Y.1    Tokunaga, F.2    Chiba, T.3    Iwai, K.4    Tanaka, K.5    Tai, T.6
  • 35
    • 11844263929 scopus 로고    scopus 로고
    • A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting
    • Richly, H.; Rape, M.; Braun, S.; Rumpf, S.; Hoege, C.; Jentsch, S. A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting. Cell, 2005, 120, 73-84.
    • (2005) Cell , vol.120 , pp. 73-84
    • Richly, H.1    Rape, M.2    Braun, S.3    Rumpf, S.4    Hoege, C.5    Jentsch, S.6
  • 36
    • 35649014889 scopus 로고    scopus 로고
    • Inaugural Article: Structure and function of the yeast U-box-containing ubiquitin ligase Ufd2p
    • Tu, D.; Li, W.; Ye, Y.; Brunger, A. T. Inaugural Article: Structure and function of the yeast U-box-containing ubiquitin ligase Ufd2p. Proc. Natl. Acad. Sci. USA, 2007, 104, 15599-15606.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 15599-15606
    • Tu, D.1    Li, W.2    Ye, Y.3    Brunger, A.T.4
  • 37
    • 37649025515 scopus 로고    scopus 로고
    • Dissecting the ER-associated degradation of a misfolded polytopic membrane protein
    • Nakatsukasa, K.; Huyer, G.; Michaelis, S.; Brodsky, J. L. Dissecting the ER-associated degradation of a misfolded polytopic membrane protein. Cell, 2008, 132, 101-112.
    • (2008) Cell , vol.132 , pp. 101-112
    • Nakatsukasa, K.1    Huyer, G.2    Michaelis, S.3    Brodsky, J.L.4
  • 39
    • 33947243954 scopus 로고    scopus 로고
    • A ubiquitin ligase transfers preformed polyubiquitin chains from a conjugating enzyme to a substrate
    • Li, W.; Tu, D.; Brunger, A. T.; Ye, Y. A ubiquitin ligase transfers preformed polyubiquitin chains from a conjugating enzyme to a substrate. Nature, 2007, 446, 333-337.
    • (2007) Nature , vol.446 , pp. 333-337
    • Li, W.1    Tu, D.2    Brunger, A.T.3    Ye, Y.4
  • 40
    • 62649096662 scopus 로고    scopus 로고
    • Mechanistic insights into active site-associated polyubiquitination by the ubiquitin-conjugating enzyme Ube2g2
    • Li, W.; Tu, D.; Li, L.; Wollert, T.; Ghirlando, R.; Brunger, A. T.; Ye, Y. Mechanistic insights into active site-associated polyubiquitination by the ubiquitin-conjugating enzyme Ube2g2. Proc. Natl. Acad. Sci. USA, 2009, 106, 3722-3727.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 3722-3727
    • Li, W.1    Tu, D.2    Li, L.3    Wollert, T.4    Ghirlando, R.5    Brunger, A.T.6    Ye, Y.7
  • 42
    • 0031038169 scopus 로고    scopus 로고
    • Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome
    • Lam, Y. A.; Xu, W.; DeMartino, G. N.; Cohen, R. E. Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome. Nature, 1997, 385, 737-740.
    • (1997) Nature , vol.385 , pp. 737-740
    • Lam, Y.A.1    Xu, W.2    DeMartino, G.N.3    Cohen, R.E.4
  • 44
    • 0037179694 scopus 로고    scopus 로고
    • A cryptic protease couples deubiquitination and degradation by the proteasome
    • Yao, T.; Cohen, R. E. A cryptic protease couples deubiquitination and degradation by the proteasome. Nature, 2002, 419, 403-407.
    • (2002) Nature , vol.419 , pp. 403-407
    • Yao, T.1    Cohen, R.E.2
  • 45
    • 1542344435 scopus 로고    scopus 로고
    • Proteasomes and their kin: Proteases in the machine age
    • Pickart, C. M.; Cohen, R. E. Proteasomes and their kin: proteases in the machine age. Nat. Rev. Mol. Cell Biol., 2004, 5, 177-187.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 177-187
    • Pickart, C.M.1    Cohen, R.E.2
  • 46
    • 33748988214 scopus 로고    scopus 로고
    • Regulation of retrotranslocation by p97-associated deubiquitinating enzyme ataxin-3
    • Wang, Q.; Li, L.; Ye, Y. Regulation of retrotranslocation by p97-associated deubiquitinating enzyme ataxin-3. J. Cell Biol., 2006, 174, 963-971.
    • (2006) J. Cell Biol. , vol.174 , pp. 963-971
    • Wang, Q.1    Li, L.2    Ye, Y.3
  • 47
    • 70349778618 scopus 로고    scopus 로고
    • The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER
    • Ernst, R.; Mueller, B.; Ploegh, H. L.; Schlieker, C. The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER. Mol. Cell, 2009, 36, 28-38.
    • (2009) Mol. Cell , vol.36 , pp. 28-38
    • Ernst, R.1    Mueller, B.2    Ploegh, H.L.3    Schlieker, C.4
  • 49
    • 33749236210 scopus 로고    scopus 로고
    • Diverse functions with a common regulator: Ubiquitin takes command of an AAA ATPase
    • Ye, Y. Diverse functions with a common regulator: ubiquitin takes command of an AAA ATPase. J. Struct. Biol., 2006, 156, 29-40.
    • (2006) J. Struct. Biol. , vol.156 , pp. 29-40
    • Ye, Y.1
  • 50
    • 1642309633 scopus 로고    scopus 로고
    • Molecular perspectives on p97-VCP: Progress in understanding its structure and diverse biological functions
    • Wang, Q.; Song, C.; Li, C. C. Molecular perspectives on p97-VCP: progress in understanding its structure and diverse biological functions. J. Struct. Biol., 2004, 146, 44-57.
    • (2004) J. Struct. Biol. , vol.146 , pp. 44-57
    • Wang, Q.1    Song, C.2    Li, C.C.3
  • 51
    • 49249130739 scopus 로고    scopus 로고
    • UBX domain proteins: Major regulators of the AAA ATPase Cdc48/p97
    • Schuberth, C.; Buchberger, A. UBX domain proteins: major regulators of the AAA ATPase Cdc48/p97. Cell Mol. Life Sci., 2008, 65, 2360-2371.
    • (2008) Cell Mol. Life Sci. , vol.65 , pp. 2360-2371
    • Schuberth, C.1    Buchberger, A.2
  • 52
    • 21744460209 scopus 로고    scopus 로고
    • Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites
    • Park, S.; Isaacson, R.; Kim, H. T.; Silver, P. A.; Wagner, G. Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites. Structure, 2005, 13, 995-1005.
    • (2005) Structure , vol.13 , pp. 995-1005
    • Park, S.1    Isaacson, R.2    Kim, H.T.3    Silver, P.A.4    Wagner, G.5
  • 53
  • 54
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
    • Ye, Y.; Meyer, H. H.; Rapoport, T. A. The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature, 2001, 414, 652-656.
    • (2001) Nature , vol.414 , pp. 652-656
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 55
    • 0036136901 scopus 로고    scopus 로고
    • AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation
    • Rabinovich, E.; Kerem, A.; Frohlich, K. U.; Diamant, N.; Bar-Nun, S. AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation. Mol. Cell Biol., 2002, 22, 626-634.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 626-634
    • Rabinovich, E.1    Kerem, A.2    Frohlich, K.U.3    Diamant, N.4    Bar-Nun, S.5
  • 57
    • 33845939821 scopus 로고    scopus 로고
    • Cdc48 (p97): A "molecular gearbox" in the ubiquitin pathway?
    • Jentsch, S.; Rumpf, S. Cdc48 (p97): a "molecular gearbox" in the ubiquitin pathway? Trends Biochem. Sci., 2007, 32, 6-11.
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 6-11
    • Jentsch, S.1    Rumpf, S.2
  • 58
    • 33845917801 scopus 로고    scopus 로고
    • The role of a novel p97/valosin-containing protein-interacting motif of gp78 in endoplasmic reticulum-associated degradation
    • Ballar, P.; Shen, Y.; Yang, H.; Fang, S. The role of a novel p97/valosin-containing protein-interacting motif of gp78 in endoplasmic reticulum-associated degradation. J. Biol. Chem., 2006, 281, 35359-35368.
    • (2006) J. Biol. Chem. , vol.281 , pp. 35359-35368
    • Ballar, P.1    Shen, Y.2    Yang, H.3    Fang, S.4
  • 59
    • 8544263881 scopus 로고    scopus 로고
    • AAA ATPase p97/valosin-containing protein interacts with gp78, a ubiquitin ligase for endoplasmic reticulum-associated degradation
    • Zhong, X.; Shen, Y.; Ballar, P.; Apostolou, A.; Agami, R.; Fang, S. AAA ATPase p97/valosin-containing protein interacts with gp78, a ubiquitin ligase for endoplasmic reticulum-associated degradation. J. Biol. Chem., 2004, 279, 45676-45684.
    • (2004) J. Biol. Chem. , vol.279 , pp. 45676-45684
    • Zhong, X.1    Shen, Y.2    Ballar, P.3    Apostolou, A.4    Agami, R.5    Fang, S.6
  • 60
    • 0035167960 scopus 로고    scopus 로고
    • Polyubiquitination is required for US11-dependent movement of MHC class I heavy chain from endoplasmic reticulum into cytosol
    • Shamu, C. E.; Flierman, D.; Ploegh, H. L.; Rapoport, T. A.; Chau, V. Polyubiquitination is required for US11-dependent movement of MHC class I heavy chain from endoplasmic reticulum into cytosol. Mol. Biol. Cell, 2001, 12, 2546-2555.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2546-2555
    • Shamu, C.E.1    Flierman, D.2    Ploegh, H.L.3    Rapoport, T.A.4    Chau, V.5
  • 61
  • 63
    • 65849514220 scopus 로고    scopus 로고
    • SCA3: Neurological features, pathogenesis and animal models
    • Riess, O.; Rub, U.; Pastore, A.; Bauer, P.; Schols, L. SCA3: neurological features, pathogenesis and animal models. Cerebellum, 2008, 7, 125-137.
    • (2008) Cerebellum , vol.7 , pp. 125-137
    • Riess, O.1    Rub, U.2    Pastore, A.3    Bauer, P.4    Schols, L.5
  • 64
    • 0034329159 scopus 로고    scopus 로고
    • Molecular genetics: Unmasking polyglutamine triggers in neurodegenerative disease
    • Gusella, J. F.; MacDonald, M. E. Molecular genetics: unmasking polyglutamine triggers in neurodegenerative disease. Nat. Rev. Neurosci., 2000, 1, 109-115.
    • (2000) Nat. Rev. Neurosci. , vol.1 , pp. 109-115
    • Gusella, J.F.1    McDonald, M.E.2
  • 65
    • 0041563693 scopus 로고    scopus 로고
    • Domain architecture of the polyglutamine protein ataxin-3: A globular domain followed by a flexible tail
    • Masino, L.; Musi, V.; Menon, R. P.; Fusi, P.; Kelly, G.; Frenkiel, T. A.; Trottier, Y.; Pastore, A. Domain architecture of the polyglutamine protein ataxin-3: a globular domain followed by a flexible tail. FEBS Lett., 2003, 549, 21-25.
    • (2003) FEBS Lett. , vol.549 , pp. 21-25
    • Masino, L.1    Musi, V.2    Menon, R.P.3    Fusi, P.4    Kelly, G.5    Frenkiel, T.A.6    Trottier, Y.7    Pastore, A.8
  • 67
    • 0032517816 scopus 로고    scopus 로고
    • Recruitment and the role of nuclear localization in polyglutamine-mediated aggregation
    • Perez, M. K.; Paulson, H. L.; Pendse, S. J.; Saionz, S. J.; Bonini, N. M.; Pittman, R. N. Recruitment and the role of nuclear localization in polyglutamine-mediated aggregation. J. Cell Biol., 1998, 143, 1457-1470.
    • (1998) J. Cell Biol. , vol.143 , pp. 1457-1470
    • Perez, M.K.1    Paulson, H.L.2    Pendse, S.J.3    Saionz, S.J.4    Bonini, N.M.5    Pittman, R.N.6
  • 68
    • 0345099501 scopus 로고    scopus 로고
    • The polyglutamine neurodegenerative protein ataxin-3 binds polyubiquitylated proteins and has ubiquitin protease activity
    • Burnett, B.; Li, F.; Pittman, R. N. The polyglutamine neurodegenerative protein ataxin-3 binds polyubiquitylated proteins and has ubiquitin protease activity. Hum. Mol. Genet., 2003, 12, 3195-3205.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 3195-3205
    • Burnett, B.1    Li, F.2    Pittman, R.N.3
  • 70
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains: Structure and function of the deubiquitinases
    • Komander, D.; Clague, M. J.; Urbe, S. Breaking the chains: structure and function of the deubiquitinases. Nat. Rev. Mol. Cell Biol., 2009, 10, 550-563.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 550-563
    • Komander, D.1    Clague, M.J.2    Urbe, S.3
  • 71
    • 0033867992 scopus 로고    scopus 로고
    • Ataxin-3, the MJD1 gene product, interacts with the two human homologs of yeast DNA repair protein RAD23, HHR23A and HHR23B
    • Wang, G.; Sawai, N.; Kotliarova, S.; Kanazawa, I.; Nukina, N. Ataxin-3, the MJD1 gene product, interacts with the two human homologs of yeast DNA repair protein RAD23, HHR23A and HHR23B. Hum. Mol. Genet., 2000, 9, 1795-1803.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 1795-1803
    • Wang, G.1    Sawai, N.2    Kotliarova, S.3    Kanazawa, I.4    Nukina, N.5
  • 72
    • 0042691818 scopus 로고    scopus 로고
    • Ataxin-3 interactions with rad23 and valosin-containing protein and its associations with ubiquitin chains and the proteasome are consistent with a role in ubiquitin-mediated proteolysis
    • Doss-Pepe, E. W.; Stenroos, E. S.; Johnson, W. G.; Madura, K. Ataxin-3 interactions with rad23 and valosin-containing protein and its associations with ubiquitin chains and the proteasome are consistent with a role in ubiquitin-mediated proteolysis. Mol. Cell Biol., 2003, 23, 6469-6483.
    • (2003) Mol. Cell Biol. , vol.23 , pp. 6469-6483
    • Doss-Pepe, E.W.1    Stenroos, E.S.2    Johnson, W.G.3    Madura, K.4
  • 73
    • 3042764201 scopus 로고    scopus 로고
    • Multiple interactions of rad23 suggest a mechanism for ubiquitylated substrate delivery important in proteolysis
    • Kim, I.; Mi, K.; Rao, H. Multiple interactions of rad23 suggest a mechanism for ubiquitylated substrate delivery important in proteolysis. Mol. Biol. Cell, 2004, 15, 3357-3365.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3357-3365
    • Kim, I.1    Mi, K.2    Rao, H.3
  • 74
    • 3142566639 scopus 로고    scopus 로고
    • Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system
    • Verma, R.; Oania, R.; Graumann, J.; Deshaies, R. J. Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system. Cell, 2004, 118, 99-110.
    • (2004) Cell , vol.118 , pp. 99-110
    • Verma, R.1    Oania, R.2    Graumann, J.3    Deshaies, R.J.4
  • 77
    • 33747891213 scopus 로고    scopus 로고
    • Ataxin-3 binds VCP/p97 and regulates retrotranslocation of ERAD substrates
    • Zhong, X.; Pittman, R. N. Ataxin-3 binds VCP/p97 and regulates retrotranslocation of ERAD substrates. Hum. Mol. Genet., 2006, 15, 2409-2420.
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 2409-2420
    • Zhong, X.1    Pittman, R.N.2
  • 78
    • 43149099696 scopus 로고    scopus 로고
    • Inhibition of p97-dependent protein degradation by Eeyarestatin I
    • Wang, Q.; Li, L.; Ye, Y. Inhibition of p97-dependent protein degradation by Eeyarestatin I. J. Biol. Chem., 2008
    • (2008) J. Biol. Chem.
    • Wang, Q.1    Li, L.2    Ye, Y.3
  • 79
    • 78649742954 scopus 로고    scopus 로고
    • The ERAD Inhibitor Eeyarestatin I Is a Bifunctional Compound with a Membrane-Binding Domain and a p97/VCP Inhibitory Group
    • Wang, Q.; Shinkre, B. A.; Lee, J. G.; Weniger, M. A.; Liu, Y.; Chen, W.; Wiestner, A.; Trenkle, W. C.; Ye, Y. The ERAD Inhibitor Eeyarestatin I Is a Bifunctional Compound with a Membrane-Binding Domain and a p97/VCP Inhibitory Group. PLoS One, 2010, 5, e15479.
    • (2010) PLoS One , vol.5
    • Wang, Q.1    Shinkre, B.A.2    Lee, J.G.3    Weniger, M.A.4    Liu, Y.5    Chen, W.6    Wiestner, A.7    Trenkle, W.C.8    Ye, Y.9
  • 80
    • 50449107542 scopus 로고    scopus 로고
    • SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins
    • Mueller, B.; Klemm, E. J.; Spooner, E.; Claessen, J. H.; Ploegh, H. L. SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins. Proc. Natl. Acad. Sci. USA, 2008, 105, 12325-12330.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 12325-12330
    • Mueller, B.1    Klemm, E.J.2    Spooner, E.3    Claessen, J.H.4    Ploegh, H.L.5
  • 82
    • 79952280797 scopus 로고    scopus 로고
    • The Machado-Joseph disease deubiquitylase ATX-3 couples longevity and proteostasis
    • Kuhlbrodt, K.; Janiesch, P. C.; Kevei, E.; Segref, A.; Barikbin, R.; Hoppe, T. The Machado-Joseph disease deubiquitylase ATX-3 couples longevity and proteostasis. Nat. Cell Biol., 2011, 13, 273-281.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 273-281
    • Kuhlbrodt, K.1    Janiesch, P.C.2    Kevei, E.3    Segref, A.4    Barikbin, R.5    Hoppe, T.6
  • 84
    • 79953722543 scopus 로고    scopus 로고
    • Ubiquitylation in ERAD: Reversing to go forward?
    • Tsai, Y. C.; Weissman, A. M. Ubiquitylation in ERAD: reversing to go forward? PLoS Biol., 2011, 9, e1001038.
    • (2011) PLoS Biol. , vol.9
    • Tsai, Y.C.1    Weissman, A.M.2
  • 86
    • 0242573090 scopus 로고    scopus 로고
    • NSF and p97/VCP: Similar at first, different at last
    • Brunger, A. T.; DeLaBarre, B. NSF and p97/VCP: similar at first, different at last. FEBS Lett., 2003, 555, 126-133.
    • (2003) FEBS Lett. , vol.555 , pp. 126-133
    • Brunger, A.T.1    DeLaBarre, B.2
  • 87
    • 0034885052 scopus 로고    scopus 로고
    • AAA+ superfamily ATPases: Common structure--diverse function
    • Ogura, T.; Wilkinson, A. J. AAA+ superfamily ATPases: common structure--diverse function. Genes Cells, 2001, 6, 575-597.
    • (2001) Genes Cells , vol.6 , pp. 575-597
    • Ogura, T.1    Wilkinson, A.J.2
  • 88
    • 35948947822 scopus 로고    scopus 로고
    • AAA+ ATPases: Achieving diversity of function with conserved machinery
    • White, S. R.; Lauring, B. AAA+ ATPases: achieving diversity of function with conserved machinery. Traffic, 2007, 8, 1657-1667.
    • (2007) Traffic , vol.8 , pp. 1657-1667
    • White, S.R.1    Lauring, B.2
  • 89
    • 0036499973 scopus 로고    scopus 로고
    • Visualization of the ER-to-cytosol dislocation reaction of a type I membrane protein
    • Fiebiger, E.; Story, C.; Ploegh, H. L.; Tortorella, D. Visualization of the ER-to-cytosol dislocation reaction of a type I membrane protein. Embo J., 2002, 21, 1041-1053.
    • (2002) Embo J. , vol.21 , pp. 1041-1053
    • Fiebiger, E.1    Story, C.2    Ploegh, H.L.3    Tortorella, D.4
  • 90
    • 60549100850 scopus 로고    scopus 로고
    • Ubiquitination directly enhances activity of the deubiquitinating enzyme ataxin-3
    • Todi, S. V.; Winborn, B. J.; Scaglione, K. M.; Blount, J. R.; Travis, S. M.; Paulson, H. L. Ubiquitination directly enhances activity of the deubiquitinating enzyme ataxin-3. Embo J., 2009, 28, 372-382.
    • (2009) Embo J. , vol.28 , pp. 372-382
    • Todi, S.V.1    Winborn, B.J.2    Scaglione, K.M.3    Blount, J.R.4    Travis, S.M.5    Paulson, H.L.6
  • 91
    • 78649811312 scopus 로고    scopus 로고
    • Activity and cellular functions of the deubiquitinating enzyme and polyglutamine disease protein ataxin-3 are regulated by ubiquitination at lysine 117
    • Todi, S. V.; Scaglione, K. M.; Blount, J. R.; Basrur, V.; Conlon, K. P.; Pastore, A.; Elenitoba-Johnson, K.; Paulson, H. L. Activity and cellular functions of the deubiquitinating enzyme and polyglutamine disease protein ataxin-3 are regulated by ubiquitination at lysine 117. J. Biol. Chem., 2010.
    • (2010) J. Biol. Chem.
    • Todi, S.V.1    Scaglione, K.M.2    Blount, J.R.3    Basrur, V.4    Conlon, K.P.5    Pastore, A.6    Elenitoba-Johnson, K.7    Paulson, H.L.8
  • 92
    • 55549086868 scopus 로고    scopus 로고
    • The deubiquitinating enzyme ataxin-3, a polyglutamine disease protein, edits Lys63 linkages in mixed linkage ubiquitin chains
    • Winborn, B. J.; Travis, S. M.; Todi, S. V.; Scaglione, K. M.; Xu, P.; Williams, A. J.; Cohen, R. E.; Peng, J.; Paulson, H. L. The deubiquitinating enzyme ataxin-3, a polyglutamine disease protein, edits Lys63 linkages in mixed linkage ubiquitin chains. J. Biol. Chem., 2008, 283, 26436-26443.
    • (2008) J. Biol. Chem. , vol.283 , pp. 26436-26443
    • Winborn, B.J.1    Travis, S.M.2    Todi, S.V.3    Scaglione, K.M.4    Xu, P.5    Williams, A.J.6    Cohen, R.E.7    Peng, J.8    Paulson, H.L.9
  • 93
    • 79959347089 scopus 로고    scopus 로고
    • A ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble States for proteasome degradation
    • Wang, Q.; Liu, Y.; Soetandyo, N.; Baek, K.; Hegde, R.; Ye, Y. A ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble States for proteasome degradation. Mol. Cell, 2011, 42, 758-770.
    • (2011) Mol. Cell , vol.42 , pp. 758-770
    • Wang, Q.1    Liu, Y.2    Soetandyo, N.3    Baek, K.4    Hegde, R.5    Ye, Y.6
  • 95
    • 57749116408 scopus 로고    scopus 로고
    • Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity
    • Duennwald, M. L.; Lindquist, S. Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity. Genes Dev., 2008, 22, 3308-3319.
    • (2008) Genes Dev. , vol.22 , pp. 3308-3319
    • Duennwald, M.L.1    Lindquist, S.2
  • 98
    • 30744451400 scopus 로고    scopus 로고
    • Functional division of substrate processing cofactors of the ubiquitin-selective Cdc48 chaperone
    • Rumpf, S.; Jentsch, S. Functional division of substrate processing cofactors of the ubiquitin-selective Cdc48 chaperone. Mol. Cell, 2006, 21, 261-269.
    • (2006) Mol. Cell , vol.21 , pp. 261-269
    • Rumpf, S.1    Jentsch, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.