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Volumn 42, Issue 5, 2010, Pages 303-310

Tetra-glutamic acid residues adjacent to Lys248 in HMG-CoA reductase are critical for the ubiquitination mediated by gp78 and UBE2G2

Author keywords

Endoplasmic reticulum associated protein degradation (ERAD); Gp78; HMG CoA reductase; Tetra glutamic acid residue; UBE2G2

Indexed keywords

3 HYDROXY 3 METHYLGLUTARYL COENZYME A; 3-HYDROXY-3-METHYLGLUTARYL-COENZYME A; ACYL COENZYME A; AUTOCRINE MOTILITY FACTOR RECEPTOR; CYTOKINE RECEPTOR; GLUTAMIC ACID; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; LYSINE; UBE2G2 PROTEIN, HUMAN; UBIQUITIN CONJUGATING ENZYME; UBIQUITIN PROTEIN LIGASE;

EID: 77951849191     PISSN: 16729145     EISSN: 17457270     Source Type: Journal    
DOI: 10.1093/abbs/gmq022     Document Type: Article
Times cited : (18)

References (21)
  • 1
    • 0025120211 scopus 로고
    • Regulation of the mevalonate pathway
    • Goldstein JL and Brown MS. Regulation of the mevalonate pathway. Nature 1990, 343: 425-430.
    • (1990) Nature , vol.343 , pp. 425-430
    • Goldstein, J.L.1    Brown, M.S.2
  • 2
    • 0026720521 scopus 로고
    • Immunological evidence for eight spans in the membrane domain of 3-hydroxy-3-methylglutaryl coenzyme A reductase: Implications for enzyme degradation in the endoplasmic reticulum
    • Roitelman J, Olender EH, Bar-Nun S, Dunn WA, Jr and Simoni RD. Immunological evidence for eight spans in the membrane domain of 3-hydroxy-3-methylglutaryl coenzyme A reductase: implications for enzyme degradation in the endoplasmic reticulum. J Cell Biol 1992, 117: 959-973.
    • (1992) J Cell Biol , vol.117 , pp. 959-973
    • Roitelman, J.1    Olender, E.H.2    Bar-Nun, S.3    Dunn Jr., W.A.4    Simoni, R.D.5
  • 3
    • 0021856440 scopus 로고
    • Membrane-bound domain of HMG CoA reductase is required for sterol-enhanced degradation of the enzyme
    • Gil G, Faust JR, Chin DJ, Goldstein JL and Brown MS. Membrane-bound domain of HMG CoA reductase is required for sterol-enhanced degradation of the enzyme. Cell 1985, 41: 249-258.
    • (1985) Cell , vol.41 , pp. 249-258
    • Gil, G.1    Faust, J.R.2    Chin, D.J.3    Goldstein, J.L.4    Brown, M.S.5
  • 4
    • 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 and Roitelman J. The ubiquitin-proteasome pathway mediates the regulated degradation of mammalian 3-hydroxy-3-methylglutaryl-coenzyme A reductase. J Biol Chem 2000, 275: 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
  • 5
    • 0346101770 scopus 로고    scopus 로고
    • Insig-dependent ubiquitination and degradation of mammalian 3-hydroxy-3-methylglutaryl-CoA reductase stimulated by sterols and gera-nylgeraniol
    • Sever N, Song BL, Yabe D, Goldstein JL, Brown MS and DeBose-Boyd RA. Insig-dependent ubiquitination and degradation of mammalian 3-hydroxy-3- methylglutaryl-CoA reductase stimulated by sterols and gera-nylgeraniol. J Biol Chem 2003, 278: 52479-52490.
    • (2003) J Biol Chem , vol.278 , pp. 52479-52490
    • Sever, N.1    Song, B.L.2    Yabe, D.3    Goldstein, J.L.4    Brown, M.S.5    DeBose-Boyd, R.A.6
  • 6
    • 18544378347 scopus 로고    scopus 로고
    • Insig-mediated degradation of HMG CoA reductase stimulated by lanosterol, an intermediate in the synthesis of cholesterol
    • Song BL, Javitt NB and DeBose-Boyd RA. Insig-mediated degradation of HMG CoA reductase stimulated by lanosterol, an intermediate in the synthesis of cholesterol. Cell Metab 2005, 1: 179-189.
    • (2005) Cell Metab , vol.1 , pp. 179-189
    • Song, B.L.1    Javitt, N.B.2    DeBose-Boyd, R.A.3
  • 7
    • 3142654791 scopus 로고    scopus 로고
    • Ubiquitination of 3-hydroxy-3-methylglutaryl-CoA reductase in permeabilized cells mediated by cytosolic E1 and a putative membrane-bound ubiquitin ligase
    • Song BL and DeBose-Boyd RA. Ubiquitination of 3-hydroxy-3-methylglutaryl- CoA reductase in permeabilized cells mediated by cytosolic E1 and a putative membrane-bound ubiquitin ligase. J Biol Chem 2004, 279: 28798-28806.
    • (2004) J Biol Chem , vol.279 , pp. 28798-28806
    • Song, B.L.1    DeBose-Boyd, R.A.2
  • 8
    • 24944591120 scopus 로고    scopus 로고
    • Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubi-quitination to degradation of HMG CoA reductase
    • Song BL, Sever N and DeBose-Boyd RA. Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubi-quitination 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
  • 9
    • 34547464338 scopus 로고    scopus 로고
    • Ufd1 is a cofactor of gp78 and plays a key role in cholesterol metabolism by regulating the stability of HMG-CoA reductase
    • Cao J, Wang J, Qi W, Miao HH, Wang J, Ge L and DeBose-Boyd RA, et al. Ufd1 is a cofactor of gp78 and plays a key role in cholesterol metabolism by regulating the stability of HMG-CoA reductase. Cell metab 2007, 6: 115-128.
    • (2007) Cell Metab , vol.6 , pp. 115-128
    • Cao, J.1    Wang, J.2    Qi, W.3    Miao, H.H.4    Wang, J.5    Ge, L.6    DeBose-Boyd, R.A.7
  • 10
    • 0019140920 scopus 로고
    • Feedback regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in livers of mice treated with mevinolin, a competitive inhibitor of the reductase
    • Kita T, Brown MS and Goldstein JL. Feedback regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in livers of mice treated with mevinolin, a competitive inhibitor of the reductase. J Clin Invest 1980, 66: 1094-1100.
    • (1980) J Clin Invest , vol.66 , pp. 1094-1100
    • Kita, T.1    Brown, M.S.2    Goldstein, J.L.3
  • 11
    • 0020967144 scopus 로고
    • Defective lipoprotein receptors and atherosclerosis. Lessons from an animal counterpart of familial hypercho-lesterolemia
    • Goldstein JL, Kita T and Brown MS. Defective lipoprotein receptors and atherosclerosis. Lessons from an animal counterpart of familial hypercho-lesterolemia. N Engl J Med 1983, 309: 288-296.
    • (1983) N Engl J Med , vol.309 , pp. 288-296
    • Goldstein, J.L.1    Kita, T.2    Brown, M.S.3
  • 12
    • 0037245750 scopus 로고    scopus 로고
    • Accelerated degradation of HMG CoA reductase mediated by binding of insig-1 to its sterol-sensing domain
    • Sever N, Yang T, Brown MS, Goldstein JL and DeBose-Boyd RA. Accelerated degradation of HMG CoA reductase mediated by binding of insig-1 to its sterol-sensing domain. Mol cell 2003, 11: 25-33.
    • (2003) Mol Cell , vol.11 , pp. 25-33
    • Sever, N.1    Yang, T.2    Brown, M.S.3    Goldstein, J.L.4    DeBose-Boyd, R.A.5
  • 13
    • 0030854859 scopus 로고    scopus 로고
    • Identification of complexes between the COOH-terminal domains of sterol regulatory element-binding proteins (SREBPs) and SREBP cleavage-activating protein
    • Sakai J, Nohturfft A, Cheng D, Ho YK, Brown MS and Goldstein JL. Identification of complexes between the COOH-terminal domains of sterol regulatory element-binding proteins (SREBPs) and SREBP cleavage-activating protein. Biol Chem 1997, 272: 20213-20221.
    • (1997) Biol Chem , vol.272 , pp. 20213-20221
    • Sakai, J.1    Nohturfft, A.2    Cheng, D.3    Ho, Y.K.4    Brown, M.S.5    Goldstein, J.L.6
  • 14
    • 0021099685 scopus 로고
    • Regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase and its mRNA in rat liver as studied with a monoclonal antibody and a cDNA probe
    • Liscum L, Luskey KL, Chin DJ, Ho YK, Goldstein JL and Brown MS. Regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase and its mRNA in rat liver as studied with a monoclonal antibody and a cDNA probe. J Biol Chem 1983, 258: 8450-8455.
    • (1983) J Biol Chem , vol.258 , pp. 8450-8455
    • Liscum, L.1    Luskey, K.L.2    Chin, D.J.3    Ho, Y.K.4    Goldstein, J.L.5    Brown, M.S.6
  • 15
    • 0033215204 scopus 로고    scopus 로고
    • Failure to cleave sterol regulatory element-binding proteins (SREBPs) causes cholesterol auxotrophy in Chinese hamster ovary cells with genetic absence of SREBP cleavage-activating protein
    • Rawson RB, DeBose-Boyd R, Goldstein JL and Brown MS. Failure to cleave sterol regulatory element-binding proteins (SREBPs) causes cholesterol auxotrophy in Chinese hamster ovary cells with genetic absence of SREBP cleavage-activating protein. J Biol Chem 1999, 274: 28549-28556.
    • (1999) J Biol Chem , vol.274 , pp. 28549-28556
    • Rawson, R.B.1    DeBose-Boyd, R.2    Goldstein, J.L.3    Brown, M.S.4
  • 16
    • 0033231014 scopus 로고    scopus 로고
    • A 'distributed degron' allows regulated entry into the ER degradation pathway
    • Gardner RG and Hampton RY. A 'distributed degron' allows regulated entry into the ER degradation pathway. EMBO J. 1999, 18: 5994-6004.
    • (1999) EMBO J. , vol.18 , pp. 5994-6004
    • Gardner, R.G.1    Hampton, R.Y.2
  • 17
    • 0037162719 scopus 로고    scopus 로고
    • Crucial step in cholesterol homeostasis: Sterols promote binding of SCAP to INSIG-1, a membrane protein that facilitates retention of SREBPs in ER
    • Yang T, Espenshade PJ, Wright ME, Yabe D, Gong Y, Aebersold R and Goldstein JL, et al. Crucial step in cholesterol homeostasis: sterols promote binding of SCAP to INSIG-1, a membrane protein that facilitates retention of SREBPs in ER. Cell 2002, 110: 489-500.
    • (2002) Cell , vol.110 , pp. 489-500
    • Yang, T.1    Espenshade, P.J.2    Wright, M.E.3    Yabe, D.4    Gong, Y.5    Aebersold, R.6    Goldstein, J.L.7
  • 18
    • 0036792050 scopus 로고    scopus 로고
    • Insig-2, a second endoplasmic reti-culum protein that binds SCAP and blocks export of sterol regulatory element-binding proteins
    • Yabe D, Brown MS and Goldstein JL. Insig-2, a second endoplasmic reti-culum protein that binds SCAP and blocks export of sterol regulatory element-binding proteins. Proc Natl Acad Sci USA 2002, 99: 12753-12758.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 12753-12758
    • Yabe, D.1    Brown, M.S.2    Goldstein, J.L.3
  • 19
    • 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 JP, Tiwari S and Weissman AM. 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
  • 21
    • 0029159799 scopus 로고
    • Finding flexible patterns in unaligned protein sequences
    • Jonassen I, Collins JF and Higgins DG. Finding flexible patterns in unaligned protein sequences. Protein Sci 1995, 4: 1587-1595.
    • (1995) Protein Sci , vol.4 , pp. 1587-1595
    • Jonassen, I.1    Collins, J.F.2    Higgins, D.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.