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Volumn 291, Issue 26, 2016, Pages 13479-13494

Contribution of accelerated degradation to feedback regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase and cholesterol metabolism in the liver

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; CHOLESTEROL; COENZYMES; DISEASES; FEEDBACK; MAMMALS; METABOLISM; PHYSIOLOGY;

EID: 84976430986     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M116.728469     Document Type: Article
Times cited : (40)

References (35)
  • 1
    • 0025120211 scopus 로고
    • Regulation of the mevalonate pathway
    • Goldstein, J. L., and Brown, M. S. (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
  • 2
    • 0019135838 scopus 로고
    • Multivalent feedback regulation of HMG CoA reductase, a control mechanism coordinating isoprenoid synthesis and cell growth
    • Brown, M. S., and Goldstein, J. L. (1980) Multivalent feedback regulation of HMG CoA reductase, a control mechanism coordinating isoprenoid synthesis and cell growth. J. Lipid Res. 21, 505-517
    • (1980) J. Lipid Res. , vol.21 , pp. 505-517
    • Brown, M.S.1    Goldstein, J.L.2
  • 3
    • 84879588228 scopus 로고    scopus 로고
    • Controlling cholesterol synthesis beyond 3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR)
    • Sharpe, L. J., and Brown, A. J. (2013) Controlling cholesterol synthesis beyond 3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR). J. Biol. Chem. 288, 18707-18715
    • (2013) J. Biol. Chem. , vol.288 , pp. 18707-18715
    • Sharpe, L.J.1    Brown, A.J.2
  • 4
    • 44849131929 scopus 로고    scopus 로고
    • Feedback regulation of cholesterol synthesis: Sterol-accelerated ubiquitination and degradation of HMG CoA reductase
    • DeBose-Boyd, R. A. (2008) Feedback regulation of cholesterol synthesis: sterol-accelerated ubiquitination and degradation of HMG CoA reductase. Cell Res. 18, 609-621
    • (2008) Cell Res. , vol.18 , pp. 609-621
    • DeBose-Boyd, R.A.1
  • 5
    • 30344473341 scopus 로고    scopus 로고
    • Protein sensors for membrane sterols
    • Goldstein, J. L., DeBose-Boyd, R. A., and Brown, M. S. (2006) Protein sensors for membrane sterols. Cell 124, 35-46
    • (2006) Cell , vol.124 , pp. 35-46
    • Goldstein, J.L.1    DeBose-Boyd, R.A.2    Brown, M.S.3
  • 6
    • 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, M. S., Goldstein, J. L., and DeBose-Boyd, R. A. (2003) Accelerated degradation of HMG CoA reductase mediated by binding of insig-1 to its sterol-sensing domain. Mol. Cell 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
  • 7
    • 0021913335 scopus 로고
    • Domain structure of 3-hydroxy-3-methylglutaryl coenzyme A reductase, a glycoprotein of the endoplasmic reticulum
    • Liscum, L., Finer-Moore, J., Stroud, R. M., Luskey, K. L., Brown, M. S., and Goldstein, J. L. (1985) Domain structure of 3-hydroxy-3-methylglutaryl coenzyme A reductase, a glycoprotein of the endoplasmic reticulum. J. Biol. Chem. 260, 522-530
    • (1985) J. Biol. Chem. , vol.260 , pp. 522-530
    • Liscum, L.1    Finer-Moore, J.2    Stroud, R.M.3    Luskey, K.L.4    Brown, M.S.5    Goldstein, J.L.6
  • 8
    • 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, E. H., Bar-Nun, S., Dunn, W. A., Jr., and Simoni, R. D. (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.4    Simoni, R.D.5
  • 9
    • 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
    • Song, B. L., Sever, N., and DeBose-Boyd, R. A. (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
    • (2005) Mol. Cell , vol.19 , pp. 829-840
    • Song, B.L.1    Sever, N.2    DeBose-Boyd, R.A.3
  • 10
    • 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, P. C., Sguigna, P. V., and DeBose-Boyd, R. A. (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. U.S.A. 108, 20503-20508
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 20503-20508
    • Jo, Y.1    Lee, P.C.2    Sguigna, P.V.3    DeBose-Boyd, R.A.4
  • 11
    • 84864684825 scopus 로고    scopus 로고
    • Ablation of gp78 in liver improves hyperlipidemia and insulin resistance by inhibiting SREBP to decrease lipid biosynthesis
    • Liu, T. F., Tang, J. J., Li, P. S., Shen, Y., Li, J. G., Miao, H. H., Li, B. L., and Song, B. L. (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
  • 12
    • 77953530388 scopus 로고    scopus 로고
    • Sterol-induced dislocation of 3-hydroxy-3-methylglutaryl coenzyme A reductase from endoplasmic reticulum membranes into the cytosol through a subcellular compartment resembling lipid droplets
    • Hartman, I. Z., Liu, P., Zehmer, J. K., Luby-Phelps, K., Jo, Y., Anderson, R. G., and DeBose-Boyd, R. A. (2010) Sterol-induced dislocation of 3-hydroxy-3-methylglutaryl coenzyme A reductase from endoplasmic reticulum membranes into the cytosol through a subcellular compartment resembling lipid droplets. J. Biol. Chem. 285, 19288-19298
    • (2010) J. Biol. Chem. , vol.285 , pp. 19288-19298
    • Hartman, I.Z.1    Liu, P.2    Zehmer, J.K.3    Luby-Phelps, K.4    Jo, Y.5    Anderson, R.G.6    DeBose-Boyd, R.A.7
  • 13
    • 84903848172 scopus 로고    scopus 로고
    • Sequential actions of the AAA-ATPase valosin-containing protein (VCP)/p97 and the proteasome 19 S regulatory particle in sterol-accelerated, endoplasmic reticulum (ER)-associated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase
    • Morris, L. L., Hartman, I. Z., Jun, D. J., Seemann, J., and DeBose-Boyd, R. A. (2014) Sequential actions of the AAA-ATPase valosin-containing protein (VCP)/p97 and the proteasome 19 S regulatory particle in sterol-accelerated, endoplasmic reticulum (ER)-associated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase. J. Biol. Chem. 289, 19053-19066
    • (2014) J. Biol. Chem. , vol.289 , pp. 19053-19066
    • Morris, L.L.1    Hartman, I.Z.2    Jun, D.J.3    Seemann, J.4    DeBose-Boyd, R.A.5
  • 14
    • 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, P. J., Wright, M. E., Yabe, D., Gong, Y., Aebersold, R., Goldstein, J. L., and Brown, M. S. (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
    • (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    Brown, M.S.8
  • 15
    • 84925851378 scopus 로고    scopus 로고
    • A century of cholesterol and coronaries: From plaques to genes to statins
    • Goldstein, J. L., and Brown, M. S. (2015) A century of cholesterol and coronaries: from plaques to genes to statins. Cell 161, 161-172
    • (2015) Cell , vol.161 , pp. 161-172
    • Goldstein, J.L.1    Brown, M.S.2
  • 16
    • 0036251153 scopus 로고    scopus 로고
    • SREBPs: Activators of the complete program of cholesterol and fatty acid synthesis in the liver
    • Horton, J. D., Goldstein, J. L., and Brown, M. S. (2002) SREBPs: activators of the complete program of cholesterol and fatty acid synthesis in the liver. J. Clin. Invest. 109, 1125-1131
    • (2002) J. Clin. Invest. , vol.109 , pp. 1125-1131
    • Horton, J.D.1    Goldstein, J.L.2    Brown, M.S.3
  • 17
    • 0000812012 scopus 로고    scopus 로고
    • Farnesol is not the nonsterol regulator mediating degradation of HMG-CoA reductase in rat liver
    • Keller, R. K., Zhao, Z., Chambers, C., and Ness, G. C. (1996) Farnesol is not the nonsterol regulator mediating degradation of HMG-CoA reductase in rat liver. Arch. Biochem. Biophys. 328, 324-330
    • (1996) Arch. Biochem. Biophys. , vol.328 , pp. 324-330
    • Keller, R.K.1    Zhao, Z.2    Chambers, C.3    Ness, G.4
  • 18
    • 0015500577 scopus 로고
    • Turnover rate of hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase as determined by use of cycloheximide
    • Edwards, P. A., and Gould, R. G. (1972) Turnover rate of hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase as determined by use of cycloheximide. J. Biol. Chem. 247, 1520-1524
    • (1972) J. Biol. Chem. , vol.247 , pp. 1520-1524
    • Edwards, P.A.1    Gould, R.G.2
  • 19
    • 20444427254 scopus 로고    scopus 로고
    • Degradation of HMG-CoA reductase in rat liver is cholesterol and ubiquitin independent
    • Ness, G. C., and Holland, R. C. (2005) Degradation of HMG-CoA reductase in rat liver is cholesterol and ubiquitin independent. FEBS Lett. 579, 3126-3130
    • (2005) FEBS Lett. , vol.579 , pp. 3126-3130
    • Ness, G.C.1    Holland, R.C.2
  • 21
    • 0346101770 scopus 로고    scopus 로고
    • Insig-dependent ubiquitination and degradation of mammalian 3-hydroxy-3-methylglutaryl-CoA reductase stimulated by sterols and geranylgeraniol
    • Sever, N., Song, B. L., Yabe, D., Goldstein, J. L., Brown, M. S., and DeBose-Boyd, R. A. (2003) Insig-dependent ubiquitination and degradation of mammalian 3-hydroxy-3-methylglutaryl-CoA reductase stimulated by sterols and geranylgeraniol. J. Biol. Chem. 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
  • 22
    • 0027471464 scopus 로고
    • A far-downstream hepatocyte-specific control region directs expression of the linked human apolipoprotein E and C-I genes in transgenic mice
    • Simonet, W. S., Bucay, N., Lauer, S. J., and Taylor, J. M. (1993) A far-downstream hepatocyte-specific control region directs expression of the linked human apolipoprotein E and C-I genes in transgenic mice. J. Biol. Chem. 268, 8221-8229
    • (1993) J. Biol. Chem. , vol.268 , pp. 8221-8229
    • Simonet, W.S.1    Bucay, N.2    Lauer, S.J.3    Taylor, J.M.4
  • 23
    • 84893140728 scopus 로고    scopus 로고
    • Insig proteins mediate feedback inhibition of cholesterol synthesis in the intestine
    • McFarlane, M. R., Liang, G., and Engelking, L. J. (2014) Insig proteins mediate feedback inhibition of cholesterol synthesis in the intestine. J. Biol. Chem. 289, 2148-2156
    • (2014) J. Biol. Chem. , vol.289 , pp. 2148-2156
    • McFarlane, M.R.1    Liang, G.2    Engelking, L.J.3
  • 24
    • 79955406213 scopus 로고    scopus 로고
    • Membrane-associated ubiquitin ligase complex containing gp78 mediates sterol-accelerated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase
    • Jo, Y., Sguigna, P. V., and DeBose-Boyd, R. A. (2011) Membrane-associated ubiquitin ligase complex containing gp78 mediates sterol-accelerated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase. J. Biol. Chem. 286, 15022-15031
    • (2011) J. Biol. Chem. , vol.286 , pp. 15022-15031
    • Jo, Y.1    Sguigna, P.V.2    DeBose-Boyd, R.A.3
  • 25
    • 84862339778 scopus 로고    scopus 로고
    • A comprehensive method for extraction and quantitative analysis of sterols and secosteroids from human plasma
    • McDonald, J. G., Smith, D. D., Stiles, A. R., and Russell, D. W. (2012) A comprehensive method for extraction and quantitative analysis of sterols and secosteroids from human plasma. J. Lipid Res. 53, 1399-1409
    • (2012) J. Lipid Res. , vol.53 , pp. 1399-1409
    • McDonald, J.G.1    Smith, D.D.2    Stiles, A.R.3    Russell, D.W.4
  • 26
    • 84937410008 scopus 로고    scopus 로고
    • Flux analysis of cholesterol biosynthesis in vivo reveals multiple tissue and cell-type specific pathways
    • Mitsche, M. A., McDonald, J. G., Hobbs, H. H., and Cohen, J. C. (2015) Flux analysis of cholesterol biosynthesis in vivo reveals multiple tissue and cell-type specific pathways. Elife 4, e07999
    • (2015) Elife , vol.4
    • Mitsche, M.A.1    McDonald, J.G.2    Hobbs, H.H.3    Cohen, J.C.4
  • 27
    • 0029797604 scopus 로고    scopus 로고
    • Overproduction of cholesterol and fatty acids causes massive liver enlargement in transgenic mice expressing truncated SREBP-1a
    • Shimano, H., Horton, J. D., Hammer, R. E., Shimomura, I., Brown, M. S., and Goldstein, J. L. (1996) Overproduction of cholesterol and fatty acids causes massive liver enlargement in transgenic mice expressing truncated SREBP-1a. J. Clin. Invest. 98, 1575-1584
    • (1996) J. Clin. Invest. , vol.98 , pp. 1575-1584
    • Shimano, H.1    Horton, J.D.2    Hammer, R.E.3    Shimomura, I.4    Brown, M.S.5    Goldstein, J.L.6
  • 28
    • 4644243461 scopus 로고    scopus 로고
    • Ubiquitin is conjugated by membrane ubiquitin ligase to three sites, including the N terminus, in transmembrane region of mammalian 3-hydroxy-3-methylglutaryl coenzyme A reductase: Implications for sterol-regulated enzyme degradation
    • Doolman, R., Leichner, G. S., Avner, R., and Roitelman, J. (2004) Ubiquitin is conjugated by membrane ubiquitin ligase to three sites, including the N terminus, in transmembrane region of mammalian 3-hydroxy-3-methylglutaryl coenzyme A reductase: implications for sterol-regulated enzyme degradation. J. Biol. Chem. 279, 38184-38193
    • (2004) J. Biol. Chem. , vol.279 , pp. 38184-38193
    • Doolman, R.1    Leichner, G.S.2    Avner, R.3    Roitelman, J.4
  • 30
    • 2142751644 scopus 로고    scopus 로고
    • Overexpression of Insig-1 in the livers of transgenic mice inhibits SREBP processing and reduces insulin-stimulated lipogenesis
    • Engelking, L. J., Kuriyama, H., Hammer, R. E., Horton, J. D., Brown, M. S., Goldstein, J. L., and 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
    • (2004) J. Clin. Invest. , vol.113 , 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
  • 31
    • 0035852770 scopus 로고    scopus 로고
    • Expression of sterol regulatory element-binding protein 1c (SREBP-1c) mRNA in rat hepatoma cells requires endogenous LXR ligands
    • DeBose-Boyd, R. A., Ou, J., Goldstein, J. L., and Brown, M. S. (2001) Expression of sterol regulatory element-binding protein 1c (SREBP-1c) mRNA in rat hepatoma cells requires endogenous LXR ligands. Proc. Natl. Acad. Sci. U.S.A. 98, 1477-1482
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 1477-1482
    • DeBose-Boyd, R.A.1    Ou, J.2    Goldstein, J.L.3    Brown, M.S.4
  • 32
    • 0037453007 scopus 로고    scopus 로고
    • Liver-specific mRNA for Insig-2 down-regulated by insulin: Implications for fatty acid synthesis
    • Yabe, D., Komuro, R., Liang, G., Goldstein, J. L., and Brown, M. S. (2003) Liver-specific mRNA for Insig-2 down-regulated by insulin: implications for fatty acid synthesis. Proc. Natl. Acad. Sci. U.S.A. 100, 3155-3160
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 3155-3160
    • Yabe, D.1    Komuro, R.2    Liang, G.3    Goldstein, J.L.4    Brown, M.S.5
  • 33
    • 33748297599 scopus 로고    scopus 로고
    • Severe facial clefting in Insig-deficient mouse embryos caused by sterol accumulation and reversed by lovastatin
    • Engelking, L. J., Evers, B. M., Richardson, J. A., Goldstein, J. L., Brown, M. S., and Liang, G. (2006) Severe facial clefting in Insig-deficient mouse embryos caused by sterol accumulation and reversed by lovastatin. J. Clin. Invest. 116, 2356-2365
    • (2006) J. Clin. Invest. , vol.116 , pp. 2356-2365
    • Engelking, L.J.1    Evers, B.M.2    Richardson, J.A.3    Goldstein, J.L.4    Brown, M.S.5    Liang, G.6
  • 34
    • 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, M. S., and Goldstein, J. L. (1980) 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. 66, 1094-1100
    • (1980) J. Clin. Invest. , vol.66 , pp. 1094-1100
    • Kita, T.1    Brown, M.S.2    Goldstein, J.L.3


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