메뉴 건너뛰기




Volumn 11, Issue 1, 2003, Pages 25-33

Accelerated degradation of HMG CoA reductase mediated by binding of insig-1 to its sterol-sensing domain

Author keywords

[No Author keywords available]

Indexed keywords

2 HYDROXYPROPYL BETA CYCLODEXTRIN; COMPACTIN; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; MEVALONIC ACID; PROTEIN; PROTEIN INSIG 1; STEROL; STEROL REGULATORY ELEMENT BINDING PROTEIN; STEROL REGULATORY ELEMENT BINDING PROTEIN CLEAVAGE ACTIVATING PROTEIN; UNCLASSIFIED DRUG;

EID: 0037245750     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(02)00822-5     Document Type: Article
Times cited : (303)

References (39)
  • 2
    • 0029927738 scopus 로고    scopus 로고
    • Heart attacks: Gone with the century?
    • Brown M.S., Goldstein J.L. Heart attacks. gone with the century? Science. 272:1996;629.
    • (1996) Science , vol.272 , pp. 629
    • Brown, M.S.1    Goldstein, J.L.2
  • 3
    • 0030941803 scopus 로고    scopus 로고
    • The SREBP pathway: Regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor
    • Brown M.S., Goldstein J.L. The SREBP pathway. regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor Cell. 89:1997;331-340.
    • (1997) Cell , vol.89 , pp. 331-340
    • Brown, M.S.1    Goldstein, J.L.2
  • 4
    • 0033613147 scopus 로고    scopus 로고
    • A proteolytic pathway that controls the cholesterol content of membranes, cells, and blood
    • Brown M.S., Goldstein J.L. A proteolytic pathway that controls the cholesterol content of membranes, cells, and blood. Proc. Natl. Acad. Sci. USA. 96:1999;11041-11048.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11041-11048
    • Brown, M.S.1    Goldstein, J.L.2
  • 6
    • 0034611014 scopus 로고    scopus 로고
    • Regulation of HMG-CoA reductase degradation requires the P-type ATPase Cod1p/Spf1p
    • Cronin S.R., Khoury A., Ferry D.K., Hampton R.Y. Regulation of HMG-CoA reductase degradation requires the P-type ATPase Cod1p/Spf1p. J. Cell Biol. 148:2000;915-924.
    • (2000) J. Cell Biol. , vol.148 , pp. 915-924
    • Cronin, S.R.1    Khoury, A.2    Ferry, D.K.3    Hampton, R.Y.4
  • 7
    • 0033599028 scopus 로고    scopus 로고
    • Transport-dependent proteolysis of SREBP: Relocation of Site-1 protease from Golgi to ER obviates the need for SREBP transport to Golgi
    • DeBose-Boyd R.A., Brown M.S., Li W.-P., Nohturfft A., Goldstein J.L., Espenshade P.J. Transport-dependent proteolysis of SREBP. relocation of Site-1 protease from Golgi to ER obviates the need for SREBP transport to Golgi Cell. 99:1999;703-712.
    • (1999) Cell , vol.99 , pp. 703-712
    • DeBose-Boyd, R.A.1    Brown, M.S.2    Li, W.-P.3    Nohturfft, A.4    Goldstein, J.L.5    Espenshade, P.J.6
  • 8
    • 0015500577 scopus 로고
    • Turnover rate of hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase as determined by use of cycloheximide
    • Edwards P.A., Gould R.G. Turnover rate of hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase as determined by use of cycloheximide. J. Biol. Chem. 247:1972;l520-l524.
    • (1972) J. Biol. Chem. , vol.247
    • Edwards, P.A.1    Gould, R.G.2
  • 9
    • 0020619724 scopus 로고
    • Mevalonolactone inhibits the rate of synthesis and enhances the rate of degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in rat hepatocytes
    • Edwards P.A., Lan S.-F., Tanaka R.D., Fogelman A.M. Mevalonolactone inhibits the rate of synthesis and enhances the rate of degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in rat hepatocytes. J. Biol. Chem. 258:1983;7272-7275.
    • (1983) J. Biol. Chem. , vol.258 , pp. 7272-7275
    • Edwards, P.A.1    Lan, S.-F.2    Tanaka, R.D.3    Fogelman, A.M.4
  • 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-l cells
    • Faust J.R., Luskey K.L., Chin D.J., Goldstein J.L., Brown M.S. Regulation of synthesis and degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase by low density lipoprotein and 25-hydroxycholesterol in UT-l cells. Proc. Natl. Acad. Sci. USA. 79:1982;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
    • 0033615648 scopus 로고    scopus 로고
    • A highly conserved signal controls degradation of 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase in eukaryotes
    • Gardner R.G., Hampton R.Y. A highly conserved signal controls degradation of 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase in eukaryotes. J. Biol. Chem. 274:1999;31671-31678.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31671-31678
    • Gardner, R.G.1    Hampton, R.Y.2
  • 12
    • 0021856440 scopus 로고
    • Membrane-bound domain of HMG CoA reductase is required for sterol-enhanced degradation of the enzyme
    • Gil G., Faust J.R., Chin D.J., Goldstein J.L., Brown M.S. Membrane-bound domain of HMG CoA reductase is required for sterol-enhanced degradation of the enzyme. Cell. 41:1985;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
  • 13
    • 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
  • 14
    • 0020973547 scopus 로고
    • Receptor-mediated endocytosis of LDL in cultured cells
    • Goldstein J.L., Basu S.K., Brown M.S. Receptor-mediated endocytosis of LDL in cultured cells. Methods Enzymol. 98:1983;241-260.
    • (1983) Methods Enzymol. , vol.98 , pp. 241-260
    • Goldstein, J.L.1    Basu, S.K.2    Brown, M.S.3
  • 15
    • 0037082099 scopus 로고    scopus 로고
    • Mutant mammalian cells as tools to delineate the sterol regulatory element-binding protein pathway for feedback regulation of lipid synthesis
    • Goldstein J.L., Rawson R.B., Brown M.S. Mutant mammalian cells as tools to delineate the sterol regulatory element-binding protein pathway for feedback regulation of lipid synthesis. Arch. Biochem. Biophys. 397:2002;139-148.
    • (2002) Arch. Biochem. Biophys. , vol.397 , pp. 139-148
    • Goldstein, J.L.1    Rawson, R.B.2    Brown, M.S.3
  • 16
    • 0031898661 scopus 로고    scopus 로고
    • Genetic analysis of hydroxymethylglutaryl-coenzyme A reductase regulated degradation
    • Hampton R.Y. Genetic analysis of hydroxymethylglutaryl-coenzyme A reductase regulated degradation. Curr. Opin. Lipidol. 9:1998;93-97.
    • (1998) Curr. Opin. Lipidol. , vol.9 , pp. 93-97
    • Hampton, R.Y.1
  • 17
    • 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
  • 18
    • 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 R.Y., Gardner R.G., Rine J. 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. 7:1996;2029-2044.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 2029-2044
    • Hampton, R.Y.1    Gardner, R.G.2    Rine, J.3
  • 19
    • 0030298339 scopus 로고    scopus 로고
    • Sterol resistance in CHO cells traced to point mutation in SREBP cleavage activating protein (SCAP)
    • Hua X., Nohturfft A., Goldstein J.L., Brown M.S. Sterol resistance in CHO cells traced to point mutation in SREBP cleavage activating protein (SCAP). Cell. 87:1996;415-426.
    • (1996) Cell , vol.87 , pp. 415-426
    • Hua, X.1    Nohturfft, A.2    Goldstein, J.L.3    Brown, M.S.4
  • 20
    • 0036790994 scopus 로고    scopus 로고
    • The hypocholesterolemic agent LY295427 up-regulates INSIG-1, identifying the INSIG-1 protein as a mediator of cholesterol homeostasis through SREBP
    • Janowski B.A. The hypocholesterolemic agent LY295427 up-regulates INSIG-1, identifying the INSIG-1 protein as a mediator of cholesterol homeostasis through SREBP. Proc. Natl. Acad. Sci. USA. 99:2002;12675-12680.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12675-12680
    • Janowski, B.A.1
  • 22
    • 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., Goldstein J.L. 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. 66:1980;1094-1100.
    • (1980) J. Clin. Invest. , vol.66 , pp. 1094-1100
    • Kita, T.1    Brown, M.S.2    Goldstein, J.L.3
  • 23
    • 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 K.L., Chin D.J., Ho Y.K., Goldstein J.L., Brown M.S. 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. 258:1983;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
  • 24
    • 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., Goldstein J.L. Domain structure of 3-hydroxy-3-methylglutaryl coenzyme A reductase, a glycoprotein of the endoplasmic reticulum. J. Biol. Chem. 260:1985;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
  • 25
    • 0002255224 scopus 로고    scopus 로고
    • Drug therapy for hypercholesterolemia and dyslipidemia
    • J.G. Hardman, L.E. Limbird, & A.G. Gilman. New York: McGraw-Hill. 971-1002.pp
    • Mahley R.W., Bersot T.P. Drug therapy for hypercholesterolemia and dyslipidemia. Hardman J.G., Limbird L.E., Gilman A.G. Goodman and Gilman's The Pharmacological Basis of Therapeutics. 2001;McGraw-Hill, New York. 971-1002.pp.
    • (2001) Goodman and Gilman's The Pharmacological Basis of Therapeutics
    • Mahley, R.W.1    Bersot, T.P.2
  • 26
    • 0029837381 scopus 로고    scopus 로고
    • Degradation of 3-hydroxy-3methylglutaryl-CoA reductase in endoplasmic reticulum membranes is accelerated as a result of increased susceptibility to proteolysis
    • McGee T.P., Cheng H.H., Kumagai H., Omura S., Simoni R.D. Degradation of 3-hydroxy-3methylglutaryl-CoA reductase in endoplasmic reticulum membranes is accelerated as a result of increased susceptibility to proteolysis. J. Biol. Chem. 271:1996;25630-25638.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25630-25638
    • McGee, T.P.1    Cheng, H.H.2    Kumagai, H.3    Omura, S.4    Simoni, R.D.5
  • 27
    • 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 J.L., Brown M.S. 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. 263:1988;8929-8937.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8929-8937
    • Nakanishi, M.1    Goldstein, J.L.2    Brown, M.S.3
  • 28
    • 0032573056 scopus 로고    scopus 로고
    • Sterols regulate processing of carbohydrate chains of wild-type SREBP cleavage-activating protein (SCAP), but not sterol-resistant mutants Y298C or D443N
    • Nohturfft A., Brown M.S., Goldstein J.L. Sterols regulate processing of carbohydrate chains of wild-type SREBP cleavage-activating protein (SCAP), but not sterol-resistant mutants Y298C or D443N. Proc. Natl. Acad. Sci. USA. 95:1998;12848-12853.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12848-12853
    • Nohturfft, A.1    Brown, M.S.2    Goldstein, J.L.3
  • 29
    • 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
  • 30
    • 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 R.B., DeBose-Boyd R., Goldstein J.L., Brown M.S. 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. 274:1999;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
  • 31
    • 0029976872 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: High level expression of a synthetic bovine opsin gene and its mutants in stable mammalian cell lines
    • Reeves P.J., Thurmond R.L., Khorana H.G. Structure and function in rhodopsin. high level expression of a synthetic bovine opsin gene and its mutants in stable mammalian cell lines Proc. Natl. Acad. Sci. USA. 93:1996;11487-11492.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11487-11492
    • Reeves, P.J.1    Thurmond, R.L.2    Khorana, H.G.3
  • 32
    • 0026461126 scopus 로고
    • Distinct sterol and nonsterol signals for the regulated degradation of 3-hydroxy-3-methylglutaryl-CoA reductase
    • Roitelman J., Simoni R.D. Distinct sterol and nonsterol signals for the regulated degradation of 3-hydroxy-3-methylglutaryl-CoA reductase. J. Biol. Chem. 267:1992;25264-25273.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25264-25273
    • Roitelman, J.1    Simoni, R.D.2
  • 33
    • 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., Simoni R.D. 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. 117:1992;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., Jr.4    Simoni, R.D.5
  • 34
    • 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 (SCAP)
    • Sakai J., Nohturfft A., Cheng D., Ho Y.K., Brown M.S., Goldstein J.L. Identification of complexes between the COOH-terminal domains of sterol regulatory element binding proteins (SREBPs) and SREBP cleavage-activating protein (SCAP). J. Biol. Chem. 272:1997;20213-20221.
    • (1997) J. 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
  • 35
    • 0342912311 scopus 로고
    • Hydroxymethylglutaryl-coenzyme A reductase-containing hepatocytes are distributed periportally in normal and mevinolin-treated rat livers
    • Singer I.I., Kawka D.W., Kazazis D.M., Alberts A.W., Chen J.S., Huff J.W., Ness G.C. Hydroxymethylglutaryl-coenzyme A reductase-containing hepatocytes are distributed periportally in normal and mevinolin-treated rat livers. Proc. Natl. Acad. Sci. USA. 81:1984;5556-5560.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 5556-5560
    • Singer, I.I.1    Kawka, D.W.2    Kazazis, D.M.3    Alberts, A.W.4    Chen, J.S.5    Huff, J.W.6    Ness, G.C.7
  • 36
    • 0024287649 scopus 로고
    • The membrane domain of 3-hydroxy-3-methylglutaryl-coenzyme A reductase confers endoplasmic reticulum localization and sterol-regulated degradation onto β-galactosidase
    • Skalnik D.G., Narita H., Kent C., Simoni R.D. The membrane domain of 3-hydroxy-3-methylglutaryl-coenzyme A reductase confers endoplasmic reticulum localization and sterol-regulated degradation onto β-galactosidase. J. Biol. Chem. 263:1988;6836-6841.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6836-6841
    • Skalnik, D.G.1    Narita, H.2    Kent, C.3    Simoni, R.D.4
  • 37
    • 0020420335 scopus 로고
    • Posttranslational processing of the LDL receptor and its genetic disruption in familial hypercholesterolemia
    • Tolleshaug H., Goldstein J.L., Schneider W.J., Brown M.S. Posttranslational processing of the LDL receptor and its genetic disruption in familial hypercholesterolemia. Cell. 30:1982;715-724.
    • (1982) Cell , vol.30 , pp. 715-724
    • Tolleshaug, H.1    Goldstein, J.L.2    Schneider, W.J.3    Brown, M.S.4
  • 38
    • 0036792050 scopus 로고    scopus 로고
    • Insig-2, a second endoplasmic reticulum protein that binds SCAP and blocks export of sterol regulatory element-binding proteins
    • Yabe D., Brown M.S., Goldstein J.L. Insig-2, a second endoplasmic reticulum protein that binds SCAP and blocks export of sterol regulatory element-binding proteins. Proc. Natl. Acad. Sci. USA. 99:2002;12753-12758.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12753-12758
    • Yabe, D.1    Brown, M.S.2    Goldstein, J.L.3
  • 39
    • 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., Brown M.S. Crucial step in cholesterol homeostasis. sterols promote binding of SCAP to INSIG-1, a membrane protein that facilitates retention of SREBPs in ER Cell. 110:2002;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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.