메뉴 건너뛰기




Volumn 23, Issue 23, 2012, Pages 4484-4494

Differential regulation of HMG-CoA reductase and Insig-1 by enzymes of the ubiquitin-proteasome system

Author keywords

[No Author keywords available]

Indexed keywords

HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; PROTEASOME; PROTEIN; PROTEIN INSIG 1; STEROL; UBIQUITIN; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 84870495262     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E12-08-0631     Document Type: Article
Times cited : (64)

References (57)
  • 1
    • 0017894322 scopus 로고
    • Induction of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in human fibroblasts incubated with compactin (ML-236B), a competitive inhibitor of the reductase
    • Brown MS, Faust JR, Goldstein JL, Kaneko I, Endo A (1978). Induction of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in human fibroblasts incubated with compactin (ML-236B), a competitive inhibitor of the reductase. J Biol Chem 253, 1121-1128. (Pubitemid 8288831)
    • (1978) Journal of Biological Chemistry , vol.253 , Issue.4 , pp. 1121-1128
    • Brown, M.S.1    Faust, J.R.2    Goldstein, J.L.3
  • 2
    • 0019135838 scopus 로고
    • Multivalent feedback regulation of HMG CoA reductase, a control mechanism coordinating isoprenoid synthesis and cell growth
    • Brown MS, Goldstein JL (1980). Multivalent feedback regulation of HMG CoA reductase, a control mechanism coordinating isoprenoid synthesis and cell growth. J Lipid Res 21, 505-517. (Pubitemid 11194847)
    • (1980) Journal of Lipid Research , vol.21 , Issue.5 , pp. 505-517
    • Brown, M.S.1    Goldstein, J.L.2
  • 4
    • 35548935098 scopus 로고    scopus 로고
    • SUMO-Specific Protease 1 Is Essential for Stabilization of HIF1α during Hypoxia
    • DOI 10.1016/j.cell.2007.08.045, PII S0092867407011439
    • Cheng J, Kang X, Zhang S, Yeh ET (2007). SUMO-specific protease 1 is essential for stabilization of HIF1alpha during hypoxia. Cell 131, 584-595. (Pubitemid 350007694)
    • (2007) Cell , vol.131 , Issue.3 , pp. 584-595
    • Cheng, J.1    Kang, X.2    Zhang, S.3    Yeh, E.T.H.4
  • 5
    • 0025649280 scopus 로고
    • The regulated degradation of 3-hydroxy-3-methylglutaryl-CoA reductase requires a short-lived protein and occurs in the endoplasmic reticulum
    • Chun KT, Bar-Nun S, Simoni RD (1990). The regulated degradation of 3-hydroxy-3-methylglutaryl-CoA reductase requires a short-lived protein and occurs in the endoplasmic reticulum. J Biol Chem 265, 22004-22010. (Pubitemid 120014256)
    • (1990) Journal of Biological Chemistry , vol.265 , Issue.35 , pp. 22004-22010
    • Chun, K.T.1    Bar-Nun, S.2    Simoni, R.D.3
  • 7
  • 8
    • 0021042806 scopus 로고
    • Alterations in the rates of synthesis and degradation of rat liver 3-hydroxy-3-methylglutaryl coenzyme A reductase produced by cholestyramine and mevinolin
    • Edwards PA, Lan SF, Fogelman AM (1983). Alterations in the rates of synthesis and degradation of rat liver 3-hydroxy-3-methylglutaryl coenzyme A reductase produced by cholestyramine and mevinolin. J Biol Chem 258, 10219-10222. (Pubitemid 14241176)
    • (1983) Journal of Biological Chemistry , vol.258 , Issue.17 , pp. 10219-10222
    • Edwards, P.A.1    Lan, S.F.2    Fogelman, A.M.3
  • 9
    • 2142751644 scopus 로고    scopus 로고
    • Overexpression of Insig-1 in the livers of transgenic mice inhibits SREBP processing and reduces insulin-stimulated lipogenesis
    • DOI 10.1172/JCI200420978
    • Engelking LJ, Kuriyama H, Hammer RE, Horton JD, Brown MS, Goldstein JL, Liang G (2004). Overexpression of Insig-1 in the livers of transgenic mice inhibits SREBP processing and reduces insulin-stimulated lipogenesis. J Clin Invest 113, 1168-1175. (Pubitemid 38544102)
    • (2004) Journal of Clinical Investigation , vol.113 , Issue.8 , pp. 1168-1175
    • Engelking, L.J.1    Kuriyama, H.2    Hammer, R.E.3    Horton, J.D.4    Brown, M.S.5    Goldstein, J.L.6    Liang, G.7
  • 10
    • 0020183575 scopus 로고
    • Regulation of synthesis and degradation of 3-hydroxy-3-methylglutaryl- coenzyme A reductase by low density lipoprotein and 25-hydroxycholesterol in UT-1 cells
    • Faust JR, Luskey KL, Chin DJ, Goldstein JL, Brown MS (1982). Regulation of synthesis and degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase by low density lipoprotein and 25-hydroxycholesterol in UT-1 cells. Proc Natl Acad Sci USA 79, 5205-5209.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 5205-5209
    • Faust, J.R.1    Luskey, K.L.2    Chin, D.J.3    Goldstein, J.L.4    Brown, M.S.5
  • 11
    • 0020973547 scopus 로고
    • Receptor-mediated endocytosis of low-density lipoprotein in cultured cells
    • Goldstein JL, Basu SK, Brown MS (1983). Receptor-mediated endocytosis of low-density lipoprotein in cultured cells. Methods Enzymol 98, 241-260. (Pubitemid 14219888)
    • (1983) Methods in Enzymology , vol.VOL. 98 , pp. 241-260
    • Goldstein, J.L.1    Basu, S.K.2    Brown, M.S.3
  • 12
    • 0025120211 scopus 로고
    • Regulation of the mevalonate pathway
    • Goldstein JL, Brown MS (1990). Regulation of the mevalonate pathway. Nature 343, 425-430.
    • (1990) Nature , vol.343 , pp. 425-430
    • Goldstein, J.L.1    Brown, M.S.2
  • 14
    • 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 RY, Gardner RG, Rine J (1996). 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 7, 2029-2044. (Pubitemid 26415008)
    • (1996) Molecular Biology of the Cell , vol.7 , Issue.12 , pp. 2029-2044
    • Hampton, R.Y.1    Gardner, R.G.2    Rine, J.3
  • 15
    • 9644300910 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated protein degradation - One model fits all?
    • DOI 10.1016/j.bbamcr.2004.10.006, PII S0167488904002575, The Ubiquitin-Proteasome System
    • Hirsch C, Jarosch E, Sommer T, Wolf DH (2004). Endoplasmic reticulum-associated protein degradation - one model fits all? Biochim BiophysActa 1695, 215-223. (Pubitemid 39574975)
    • (2004) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1695 , Issue.1-3 , pp. 215-223
    • Hirsch, C.1    Jarosch, E.2    Sommer, T.3    Wolf, D.H.4
  • 16
    • 70350400757 scopus 로고    scopus 로고
    • The sterol-sensing endoplasmic reticulum (ER) membrane protein TRC8 hampers ER to Golgi transport of sterol regulatory element-binding protein-2 (SREBP-2)/SREBP cleavage-activated protein and reduces SREBP-2 cleavage
    • Irisawa M, Inoue J, Ozawa N, Mori K, Sato R (2009). The sterol-sensing endoplasmic reticulum (ER) membrane protein TRC8 hampers ER to Golgi transport of sterol regulatory element-binding protein-2 (SREBP-2)/SREBP cleavage-activated protein and reduces SREBP-2 cleavage. J Biol Chem 284, 28995-29004.
    • (2009) J Biol Chem , vol.284 , pp. 28995-29004
    • Irisawa, M.1    Inoue, J.2    Ozawa, N.3    Mori, K.4    Sato, R.5
  • 18
    • 77952860536 scopus 로고    scopus 로고
    • Control of cholesterol synthesis through regulated ER-associated degradation of HMG CoA reductase
    • Jo Y, Debose-Boyd RA (2010). Control of cholesterol synthesis through regulated ER-associated degradation of HMG CoA reductase. Crit Rev Biochem Mol Biol 45, 185-198.
    • (2010) Crit Rev Biochem Mol Biol , vol.45 , pp. 185-198
    • Jo, Y.1    Debose-Boyd, R.A.2
  • 19
    • 84855510314 scopus 로고    scopus 로고
    • Sterol-induced degradation of HMG CoA reductase depends on interplay of two Insigs and two ubiquitin ligases, gp78 and Trc8
    • Jo Y, Lee PC, Sguigna PV, DeBose-Boyd RA (2011). Sterol-induced degradation of HMG CoA reductase depends on interplay of two Insigs and two ubiquitin ligases, gp78 and Trc8. Proc Natl Acad Sci USA 108, 20503-20508.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 20503-20508
    • Jo, Y.1    Lee, P.C.2    Sguigna, P.V.3    DeBose-Boyd, R.A.4
  • 20
    • 0017807973 scopus 로고
    • Inhibitory effects on lipid metabolism in cultured cells of ML-236B, a potent inhibitor of 3-hydroxy-3-methylglutaryl-coenzyme-A reductase
    • Kaneko I, Hazama-Shimada Y, Endo A (1978). Inhibitory effects on lipid metabolism in cultured cells of ML-236B, a potent inhibitor of 3-hydroxy-3-methylglutaryl-coenzyme-A reductase. Eur J Biochem 87, 313-321. (Pubitemid 8355173)
    • (1978) European Journal of Biochemistry , vol.87 , Issue.2 , pp. 313-321
    • Kaneko, I.1    Hazama-Shimada, Y.2    Endo, A.3
  • 22
    • 36248988054 scopus 로고    scopus 로고
    • Ubiquitin ligases, critical mediators of endoplasmic reticulum-associated degradation
    • DOI 10.1016/j.semcdb.2007.09.002, PII S1084952107001486, Degredation of Misfolded Glycoproteins
    • Kostova Z, Tsai YC, Weissman AM (2007). Ubiquitin ligases, critical mediators of endoplasmic reticulum-associated degradation. Semin Cell Dev Biol 18, 770-779. (Pubitemid 350138452)
    • (2007) Seminars in Cell and Developmental Biology , vol.18 , Issue.6 , pp. 770-779
    • Kostova, Z.1    Tsai, Y.C.2    Weissman, A.M.3
  • 23
    • 33846013601 scopus 로고    scopus 로고
    • Sterol-regulated degradation of insig-1 mediated by the membrane-bound ubiquitin ligase gp78
    • DOI 10.1074/jbc.M608999200
    • Lee JN, Song B, DeBose-Boyd RA, Ye J (2006). Sterol-regulated degradation of Insig-1 mediated by the membrane-bound ubiquitin ligase gp78. J Biol Chem 281, 39308-39315. (Pubitemid 46041890)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.51 , pp. 39308-39315
    • Joon, N.L.1    Song, B.2    DeBose-Boyd, R.A.3    Ye, J.4
  • 24
    • 7244221504 scopus 로고    scopus 로고
    • Proteolytic activation of sterol regulatory element-binding protein induced by cellular stress through depletion of Insig-1
    • DOI 10.1074/jbc.M408235200
    • Lee JN, Ye J (2004). Proteolytic activation of sterol regulatory element-binding protein induced by cellular stress through depletion of Insig-1. J Biol Chem 279, 45257-45265. (Pubitemid 39430941)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.43 , pp. 45257-45265
    • Lee, J.N.1    Ye, J.2
  • 25
    • 75149146624 scopus 로고    scopus 로고
    • The TRC8 ubiquitin ligase is sterol regulated and interacts with lipid and protein biosynthetic pathways
    • Lee JP, Brauweiler A, Rudolph M, Hooper JE, Drabkin HA, Gemmill RM (2010). The TRC8 ubiquitin ligase is sterol regulated and interacts with lipid and protein biosynthetic pathways. Mol Cancer Res 8, 93-106.
    • (2010) Mol Cancer Res , vol.8 , pp. 93-106
    • Lee, J.P.1    Brauweiler, A.2    Rudolph, M.3    Hooper, J.E.4    Drabkin, H.A.5    Gemmill, R.M.6
  • 26
    • 67749116062 scopus 로고    scopus 로고
    • Dislocation of HMG-CoA reductase and Insig-1, two polytopic endoplasmic reticulum proteins, en route to proteasomal degradation
    • Leichner GS, Avner R, Harats D, Roitelman J (2009). Dislocation of HMG-CoA reductase and Insig-1, two polytopic endoplasmic reticulum proteins, en route to proteasomal degradation. Mol Biol Cell 20, 3330-3341.
    • (2009) Mol Biol Cell , vol.20 , pp. 3330-3341
    • Leichner, G.S.1    Avner, R.2    Harats, D.3    Roitelman, J.4
  • 27
    • 80052779813 scopus 로고    scopus 로고
    • Metabolically regulated endoplasmic reticulum-associated degradation of 3-hydroxy-3-methylglutaryl-CoA reductase: Evidence for requirement of a geranylgeranylated protein
    • Leichner GS, Avner R, Harats D, Roitelman J (2011). Metabolically regulated endoplasmic reticulum-associated degradation of 3-hydroxy-3- methylglutaryl-CoA reductase: evidence for requirement of a geranylgeranylated protein. J Biol Chem 286, 32150-32161.
    • (2011) J Biol Chem , vol.286 , pp. 32150-32161
    • Leichner, G.S.1    Avner, R.2    Harats, D.3    Roitelman, J.4
  • 28
    • 0021052720 scopus 로고
    • 3-Hydroxy-3-methylglutaryl-CoA reductase: A transmembrane glycoprotein of the endoplasmic reticulum with N-linked 'high-mannose' oligosaccharides
    • Liscum L, Cummings RD, Anderson RG, DeMartino GN, Goldstein JL, Brown MS (1983a). 3-Hydroxy-3-methylglutaryl-CoA reductase: a transmembrane glycoprotein of the endoplasmic reticulum with N-linked "high-mannose" oligosaccharides. Proc Natl Acad Sci USA 80,7165-7169. (Pubitemid 14207375)
    • (1983) Proceedings of the National Academy of Sciences of the United States of America , vol.80 , Issue.23 I , pp. 7165-7169
    • Liscum, L.1    Cummings, R.D.2    Anderson, R.G.W.3
  • 29
    • 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, Brown MS (1983b). 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 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
  • 30
    • 84864684825 scopus 로고    scopus 로고
    • Ablation of gp78 in liver improves hyperlipidemia and insulin resistance by inhibiting SREBP to decrease lipid biosynthesis
    • Liu TF, Tang JJ, Li PS, Shen Y, Li JG, Miao HH, Li BL, Song BL (2012). Ablation of gp78 in liver improves hyperlipidemia and insulin resistance by inhibiting SREBP to decrease lipid biosynthesis. Cell Metab 16, 213-225.
    • (2012) Cell Metab , vol.16 , pp. 213-225
    • Liu, T.F.1    Tang, J.J.2    Li, P.S.3    Shen, Y.4    Li, J.G.5    Miao, H.H.6    Li, B.L.7    Song, B.L.8
  • 31
    • 60449094498 scopus 로고    scopus 로고
    • Heart disease and stroke statistics-2009 update: A report from the American Heart Association Statistics Committee and Stroke Statistics Subcommittee
    • Lloyd-Jones D et al. (2009). Heart disease and stroke statistics-2009 update:a report from the American Heart Association Statistics Committee and Stroke Statistics Subcommittee. Circulation 119, 480-486.
    • (2009) Circulation , vol.119 , pp. 480-486
    • Lloyd-Jones, D.1
  • 32
    • 84862840315 scopus 로고    scopus 로고
    • Thymocyte responsiveness to endogenous glucocorticoids is required for immunological fitness
    • Mittelstadt PR, Monteiro JP, Ashwell JD (2012). Thymocyte responsiveness to endogenous glucocorticoids is required for immunological fitness. J Clin Invest 122, 2384-2394.
    • (2012) J Clin Invest , vol.122 , pp. 2384-2394
    • Mittelstadt, P.R.1    Monteiro, J.P.2    Ashwell, J.D.3
  • 34
    • 0023902411 scopus 로고
    • Multivalent control of 3-hydroxy-3-methylglutaryl coenzyme A reductase. Mevalonate-derived product inhibits translation of mRNA and accelerates degradation of enzyme
    • Nakanishi M, Goldstein JL, Brown MS (1988). Multivalent control of 3-hydroxy-3-methylglutaryl coenzyme A reductase. Mevalonate-derived product inhibits translation of mRNA and accelerates degradation of enzyme. J Biol Chem 263, 8929-8937.
    • (1988) J Biol Chem , vol.263 , pp. 8929-8937
    • Nakanishi, M.1    Goldstein, J.L.2    Brown, M.S.3
  • 35
    • 79953142340 scopus 로고    scopus 로고
    • A systematic search for endoplasmic reticulum (ER) membrane-associated RING finger proteins identifies Nixin/ZNRF4 as a regulator of calnexin stability and ER homeostasis
    • Neutzner A, Neutzner M, Benischke AS, Ryu SW, Frank S, Youle RJ, Karbowski M (2011). A systematic search for endoplasmic reticulum (ER) membrane-associated RING finger proteins identifies Nixin/ZNRF4 as a regulator of calnexin stability and ER homeostasis. J Biol Chem 286, 8633-8643.
    • (2011) J Biol Chem , vol.286 , pp. 8633-8643
    • Neutzner, A.1    Neutzner, M.2    Benischke, A.S.3    Ryu, S.W.4    Frank, S.5    Youle, R.J.6    Karbowski, M.7
  • 36
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB
    • DOI 10.1016/S0092-8674(94)90482-0
    • Palombella VJ, Rando OJ, Goldberg AL, Maniatis T (1994). The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B. Cell 78, 773-785. (Pubitemid 24294453)
    • (1994) Cell , vol.78 , Issue.5 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 37
    • 34547134260 scopus 로고    scopus 로고
    • SPFH2 mediates the endoplasmic reticulum-associated degradation of inositol 1,4,5-trisphosphate receptors and other substrates in mammalian cells
    • DOI 10.1074/jbc.M701862200
    • Pearce MM, Wang Y, Kelley GG, Wojcikiewicz RJ (2007). SPFH2 mediates the endoplasmic reticulum-associated degradation of inositol 1,4,5-trisphosphate receptors and other substrates in mammalian cells. J Biol Chem 282, 20104-20115. (Pubitemid 47099990)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.28 , pp. 20104-20115
    • Pearce, M.M.P.1    Wang, Y.2    Kelley, G.G.3    Wojcikiewicz, R.J.H.4
  • 38
    • 67449102905 scopus 로고    scopus 로고
    • An endoplasmic reticulum (ER) membrane complex composed of SPFH1 and SPFH2 mediates the ER-associated degradation of inositol 1,4,5-trisphosphate receptors
    • Pearce MM, Wormer DB, Wilkens S, Wojcikiewicz RJ (2009). An endoplasmic reticulum (ER) membrane complex composed of SPFH1 and SPFH2 mediates the ER-associated degradation of inositol 1,4,5-trisphosphate receptors. J Biol Chem 284, 10433-10445.
    • (2009) J Biol Chem , vol.284 , pp. 10433-10445
    • Pearce, M.M.1    Wormer, D.B.2    Wilkens, S.3    Wojcikiewicz, R.J.4
  • 39
    • 0347623204 scopus 로고    scopus 로고
    • Nonspecific, concentration-dependent stimulation and repression of mammalian gene expression by small interfering RNAs (siRNAs)
    • DOI 10.1261/rna5160904
    • Persengiev SP, Zhu X, Green MR (2004). Nonspecific, concentration- dependent stimulation and repression of mammalian gene expression by small interfering RNAs (siRNAs). RNA 10, 12-18. (Pubitemid 38018731)
    • (2004) RNA , vol.10 , Issue.1 , pp. 12-18
    • Persengiev, S.P.1    Zhu, X.2    Green, M.R.3
  • 40
    • 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 (2000). The ubiquitin-proteasome pathway mediates the regulated degradation of mammalian 3-hydroxy-3-methylglutaryl-coenzyme A reductase. J Biol Chem 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
  • 41
    • 1342346596 scopus 로고    scopus 로고
    • Apomine, a Novel Hypocholesterolemic Agent, Accelerates Degradation of 3-Hydroxy-3-methylglutaryl-coenzyme A Reductase and Stimulates Low Density Lipoprotein Receptor Activity
    • DOI 10.1074/jbc.M308094200
    • Roitelman J, Masson D, Avner R, Ammon-Zufferey C, Perez A, Guyon-Gellin Y, Bentzen CL, Niesor EJ (2004). Apomine, a novel hypocholesterolemic agent, accelerates degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase and stimulates low density lipoprotein receptor activity. J Biol Chem 279, 6465-6473. (Pubitemid 38248780)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.8 , pp. 6465-6473
    • Roitelman, J.1    Masson, D.2    Avner, R.3    Ammon-Zufferey, C.4    Perez, A.5    Guyon-Gellin, Y.6    Bentzen, C.L.7    Niesor, E.J.8
  • 42
    • 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 WAJ, Simoni RD (1992). 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 117, 959-973.
    • (1992) J Cell Biol , vol.117 , pp. 959-973
    • Roitelman, J.1    Olender, E.H.2    Bar-Nun, S.3    Dunn, W.A.J.4    Simoni, R.D.5
  • 43
    • 0026461126 scopus 로고
    • Distinct sterol and nonsterol signals for the regulated degradation of 3-hydroxy-3-methylglutaryl-CoA reductase
    • Roitelman J, Simoni RD (1992). Distinct sterol and nonsterol signals for the regulated degradation of 3-hydroxy-3-methylglutaryl-CoA reductase. J Biol Chem 267, 25264-25273.
    • (1992) J Biol Chem , vol.267 , pp. 25264-25273
    • Roitelman, J.1    Simoni, R.D.2
  • 46
    • 0346101770 scopus 로고    scopus 로고
    • Insig-dependent Ubiquitination and Degradation of Mammalian 3-Hydroxy-3-methylglutaryl-CoA Reductase Stimulated by Sterols and Geranylgeraniol
    • DOI 10.1074/jbc.M310053200
    • Sever N, Song BL, Yabe D, Goldstein JL, Brown MS, DeBose-Boyd RA (2003a). Insig-dependent ubiquitination and degradation of mammalian 3-hydroxy-3-methylglutaryl-CoA reductase stimulated by sterols and geranylgeraniol. J Biol Chem 278, 52479-52490. (Pubitemid 38035841)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.52 , pp. 52479-52490
    • Sever, N.1    Song, B.-L.2    Yabe, D.3    Goldstein, J.L.4    Brown, M.S.5    DeBose-Boydb, R.A.6
  • 47
    • 0037245750 scopus 로고    scopus 로고
    • Accelerated degradation of HMG CoA reductase mediated by binding of insig-1 to its sterol-sensing domain
    • DOI 10.1016/S1097-2765(02)00822-5
    • Sever N, Yang T, Brown MS, Goldstein JL, DeBose-Boyd RA (2003b). Accelerated degradation of HMG CoA reductase mediated by binding of insig-1 to its sterol-sensing domain. Mol Cell 11, 25-33. (Pubitemid 36126588)
    • (2003) Molecular Cell , vol.11 , Issue.1 , pp. 25-33
    • Sever, N.1    Yang, T.2    Brown, M.S.3    Goldstein, J.L.4    DeBose-Boyd, R.A.5
  • 48
    • 70449729362 scopus 로고    scopus 로고
    • Targeting of gp78 for ubiquitin-mediated proteasomal degradation by Hrd1: Cross-talk between E3s in the endoplasmic reticulum
    • Shmueli A, Tsai YC, Yang M, Braun MA, Weissman AM (2009). Targeting of gp78 for ubiquitin-mediated proteasomal degradation by Hrd1: cross-talk between E3s in the endoplasmic reticulum. Biochem Biophys Res Commun 390, 758-762.
    • (2009) Biochem Biophys Res Commun , vol.390 , pp. 758-762
    • Shmueli, A.1    Tsai, Y.C.2    Yang, M.3    Braun, M.A.4    Weissman, A.M.5
  • 49
    • 24944591120 scopus 로고    scopus 로고
    • Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase
    • DOI 10.1016/j.molcel.2005.08.009, PII S1097276505015273
    • Song BL, Sever N, DeBose-Boyd RA (2005). Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase. Mol Cell 19, 829-840. (Pubitemid 41316676)
    • (2005) Molecular Cell , vol.19 , Issue.6 , pp. 829-840
    • Song, B.-L.1    Sever, N.2    DeBose-Boyd, R.A.3
  • 50
    • 33746042622 scopus 로고    scopus 로고
    • Thematic review series: The pathogenesis of atherosclerosis. An interpretive history of the cholesterol controversy, part V: The discovery of the statins and the end of the controversy
    • Steinberg D (2006). Thematic review series: the pathogenesis of atherosclerosis. An interpretive history of the cholesterol controversy, part V: the discovery of the statins and the end of the controversy. J Lipid Res 47, 1339-1351.
    • (2006) J Lipid Res , vol.47 , pp. 1339-1351
    • Steinberg, D.1
  • 53
    • 79952844773 scopus 로고    scopus 로고
    • The unfolded protein response, degradation from endoplasmic reticulum and cancer
    • Tsai YC, Weissman AM (2010). The unfolded protein response, degradation from endoplasmic reticulum and cancer. Genes Cancer 1, 764-778.
    • (2010) Genes Cancer , vol.1 , pp. 764-778
    • Tsai, Y.C.1    Weissman, A.M.2
  • 54
    • 56749176947 scopus 로고    scopus 로고
    • One step at a time: Endoplasmic reticulum-associated degradation
    • Vembar SS, Brodsky JL (2008). One step at a time: endoplasmic reticulum-associated degradation. Nat Rev Mol Cell Biol 9, 944-957.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 944-957
    • Vembar, S.S.1    Brodsky, J.L.2
  • 55
    • 71749088921 scopus 로고    scopus 로고
    • SPFH1 and SPFH2 mediate the ubiquitination and degradation of inositol 1,4,5-trisphosphate receptors in muscarinic receptor-expressing HeLa cells
    • Wang Y et al. (2009). SPFH1 and SPFH2 mediate the ubiquitination and degradation of inositol 1,4,5-trisphosphate receptors in muscarinic receptor-expressing HeLa cells. Biochim Biophys Acta 1793, 1710-1718.
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 1710-1718
    • Wang, Y.1
  • 56
    • 20344379921 scopus 로고    scopus 로고
    • Mutation of SENP1/SuPr-2 reveals an essential role for desumoylation in mouse development
    • DOI 10.1128/MCB.25.12.5171-5182.2005
    • Yamaguchi T, Sharma P, Athanasiou M, Kumar A, Yamada S, Kuehn MR (2005). Mutation of SENP1/SuPr-2 reveals an essential role for desumoylation in mouse development. Mol Cell Biol 25, 5171-5182. (Pubitemid 40781115)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.12 , pp. 5171-5182
    • Yamaguchi, T.1    Sharma, P.2    Athanasiou, M.3    Kumar, A.4    Yamada, S.5    Kuehn, M.R.6
  • 57
    • 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
    • DOI 10.1016/S0092-8674(02)00872-3
    • Yang T, Espenshade PJ, Wright ME, Yabe D, Gong Y, Aebersold R, Goldstein JL, Brown MS (2002). Crucial step in cholesterol homeostasis: sterols promote binding of SCAP to INSIG-1, a membrane protein that facilitates retention of SREBPs in ER. Cell 110, 489-500. (Pubitemid 35232292)
    • (2002) Cell , vol.110 , Issue.4 , 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    Brown, M.S.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.