메뉴 건너뛰기




Volumn 303, Issue 1, 2003, Pages 91-97

A novel mammalian endoplasmic reticulum ubiquitin ligase homologous to the yeast Hrd1

Author keywords

Cystic fibrosis transmembrane conductance regulator; Endoplasmic reticulum associated degradation; hHrd1; HMG CoA reductase; Ubiquitin protein ligase

Indexed keywords

LIGASE; PROTEIN; PROTEIN HRD1; UBIQUITIN; UNCLASSIFIED DRUG; CFTR PROTEIN, HUMAN; COMPLEMENTARY DNA; HRD1 PROTEIN, S CEREVISIAE; RECOMBINANT PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; TRANSMEMBRANE CONDUCTANCE REGULATOR; UBIQUITIN PROTEIN LIGASE;

EID: 0037470838     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(03)00279-1     Document Type: Article
Times cited : (101)

References (26)
  • 1
    • 0036702298 scopus 로고    scopus 로고
    • ER-associated degradation in protein quality control and cellular regulation
    • Hampton R.Y. ER-associated degradation in protein quality control and cellular regulation. Curr. Opin. Cell Biol. 14:2002;476-482.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 476-482
    • Hampton, R.Y.1
  • 2
    • 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. 82:2002;373-428.
    • (2002) Physiol. Rev. , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 3
    • 0033168382 scopus 로고    scopus 로고
    • Retrograde protein translocation: Eradication of secretory proteins in health and disease
    • Plemper R.K., Wolf D.H. Retrograde protein translocation: eradication of secretory proteins in health and disease. Trends Biochem. Sci. 24:1999;266-270.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 266-270
    • Plemper, R.K.1    Wolf, D.H.2
  • 4
    • 0030695478 scopus 로고    scopus 로고
    • Pathways of ubiquitin conjugation
    • Haas A.L., Siepmann T.J. Pathways of ubiquitin conjugation. FASEB J. 11:1997;1257-1268.
    • (1997) FASEB J. , vol.11 , pp. 1257-1268
    • Haas, A.L.1    Siepmann, T.J.2
  • 5
    • 0033961923 scopus 로고    scopus 로고
    • RING for destruction?
    • Freemont P.S. RING for destruction? Curr. Biol. 10:2000;R84-R87.
    • (2000) Curr. Biol. , vol.10
    • Freemont, P.S.1
  • 7
    • 0034266806 scopus 로고    scopus 로고
    • RING finger proteins: Mediators of ubiquitin ligase activity
    • Joazeiro C., Weissman A.M. RING finger proteins: mediators of ubiquitin ligase activity. Cell. 102:2000;549-552.
    • (2000) Cell , vol.102 , pp. 549-552
    • Joazeiro, C.1    Weissman, A.M.2
  • 8
    • 0025120211 scopus 로고
    • Regulation of the mevalonate pathway
    • Goldstein J.L., Brown M.S. Regulation of the mevalonate pathway. Nature. 343:1990;425-430.
    • (1990) Nature , vol.343 , pp. 425-430
    • Goldstein, J.L.1    Brown, M.S.2
  • 9
    • 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. 94:1997;12944-12948.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12944-12948
    • Hampton, R.Y.1    Bhakta, H.2
  • 10
    • 0034680918 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway mediates the regulated degradation of mammalian 3-hydroxy-3-methylglutaryl-coenzyme A reductase
    • Ravid T., Doolman R., Avner R., Harats D., Roitelman J. The ubiquitin-proteasome pathway mediates the regulated degradation of mammalian 3-hydroxy-3-methylglutaryl-coenzyme A reductase. J. Biol. Chem. 275:2000;35840-35847.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35840-35847
    • Ravid, T.1    Doolman, R.2    Avner, R.3    Harats, D.4    Roitelman, J.5
  • 11
    • 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. 276:2001;10663-10669.
    • (2001) J. Biol. Chem. , vol.276 , pp. 10663-10669
    • Deak, P.M.1    Wolf, D.H.2
  • 12
    • 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. 3:2001;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
  • 13
    • 0032960581 scopus 로고    scopus 로고
    • A RING-H2 finger motif is essential for the function of Der3/Hrd1 in endoplasmic reticulum associated protein degradation in the yeast Saccharomyces cerevisiae
    • Bordallo J., Wolf D.H. A RING-H2 finger motif is essential for the function of Der3/Hrd1 in endoplasmic reticulum associated protein degradation in the yeast Saccharomyces cerevisiae. FEBS Lett. 448:1999;244-248.
    • (1999) FEBS Lett. , vol.448 , pp. 244-248
    • Bordallo, J.1    Wolf, D.H.2
  • 14
    • 0032957204 scopus 로고    scopus 로고
    • Biosynthesis and degradation of CFTR
    • Kopito R.R. Biosynthesis and degradation of CFTR. Physiol. Rev. 79:1999;S167-S173.
    • (1999) Physiol. Rev. , vol.79
    • Kopito, R.R.1
  • 15
    • 0037023764 scopus 로고    scopus 로고
    • A principal role for the proteasome in endoplasmic reticulum-associated degradation of misfolded intracellular cystic fibrosis transmembrane conductance regulator
    • Gelman M.S., Kannegaard E.S., Kopito R.R. A principal role for the proteasome in endoplasmic reticulum-associated degradation of misfolded intracellular cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. 277:2002;11709-11714.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11709-11714
    • Gelman, M.S.1    Kannegaard, E.S.2    Kopito, R.R.3
  • 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. 532:2002;147-152.
    • (2002) FEBS Lett. , vol.532 , pp. 147-152
    • Kaneko, M.1    Ishiguro, M.2    Niinuma, Y.3    Uesugi, M.4    Nomura, Y.5
  • 17
    • 0033591363 scopus 로고    scopus 로고
    • Identification of the ubiquitin carrier proteins, E2s, involved in signal-induced conjugation and subsequent degradation of IκBα
    • Gonen H., Bercovich B., Orian A., Carrano A., Takizawa C., Yamanaka K., Pagano M., Iwai K., Ciechanover A. Identification of the ubiquitin carrier proteins, E2s, involved in signal-induced conjugation and subsequent degradation of IκBα J. Biol. Chem. 274:1999;14823-14830.
    • (1999) J. Biol. Chem. , vol.274 , pp. 14823-14830
    • Gonen, H.1    Bercovich, B.2    Orian, A.3    Carrano, A.4    Takizawa, C.5    Yamanaka, K.6    Pagano, M.7    Iwai, K.8    Ciechanover, A.9
  • 19
    • 0020478687 scopus 로고
    • "Covalent affinity" purification of ubiquitin-activating enzyme
    • Ciechanover A., Elias S., Heller H., Hershko A. "Covalent affinity" purification of ubiquitin-activating enzyme. J. Biol. Chem. 257:1982;2537-2542.
    • (1982) J. Biol. Chem. , vol.257 , pp. 2537-2542
    • Ciechanover, A.1    Elias, S.2    Heller, H.3    Hershko, A.4
  • 20
    • 0034733717 scopus 로고    scopus 로고
    • Cystic fibrosis mutations lead to carboxyl-terminal fragments that highlight an early biogenesis step of the cystic fibrosis transmembrane conductance regulator
    • Van Oene M., Lukacs G.L., Rommens J.M. Cystic fibrosis mutations lead to carboxyl-terminal fragments that highlight an early biogenesis step of the cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. 275:2000;19577-19584.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19577-19584
    • Van Oene, M.1    Lukacs, G.L.2    Rommens, J.M.3
  • 21
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 22
    • 0035895959 scopus 로고    scopus 로고
    • Cbl-b, a RING-type E3 ubiquitin ligase, targets phosphatidylinositol 3-kinase for ubiquitination in T cells
    • Fang D., Wang H.Y., Fang N., Altman Y., Elly C., Liu Y.C. Cbl-b, a RING-type E3 ubiquitin ligase, targets phosphatidylinositol 3-kinase for ubiquitination in T cells. J. Biol. Chem. 276:2001;4872-4878.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4872-4878
    • Fang, D.1    Wang, H.Y.2    Fang, N.3    Altman, Y.4    Elly, C.5    Liu, Y.C.6
  • 24
    • 0035800802 scopus 로고    scopus 로고
    • Deletion of the Src homology 3 domain and C-terminal proline-rich sequences in Bcr-Abl prevents Abl interactor 2 degradation and spontaneous cell migration and impairs leukemogenesis
    • Dai Z., Kerzic P., Schroeder W.G., McNiece I.K. Deletion of the Src homology 3 domain and C-terminal proline-rich sequences in Bcr-Abl prevents Abl interactor 2 degradation and spontaneous cell migration and impairs leukemogenesis. J. Biol. Chem. 276:2001;28954-28960.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28954-28960
    • Dai, Z.1    Kerzic, P.2    Schroeder, W.G.3    McNiece, I.K.4
  • 25
    • 0036720843 scopus 로고    scopus 로고
    • Concerted action of ENaC, Nedd4-2, and Sgk1 in transepithelial Na(+) transport
    • Kamynina E., Staub O. Concerted action of ENaC, Nedd4-2, and Sgk1 in transepithelial Na(+) transport. Am. J. Physiol. Renal Physiol. 283:2002;F377-F387.
    • (2002) Am. J. Physiol. Renal Physiol. , vol.283
    • Kamynina, E.1    Staub, O.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.