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Volumn 10, Issue 10, 1999, Pages 3409-3423

The role of the 3-hydroxy 3-methylglutaryl coenzyme A reductase cytosolic domain in karmellae biogenesis

Author keywords

[No Author keywords available]

Indexed keywords

BETA GALACTOSIDASE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE;

EID: 0032869187     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.10.10.3409     Document Type: Article
Times cited : (26)

References (85)
  • 1
    • 0020972383 scopus 로고
    • Ultrastructural analysis of crystalloid endoplasmic reticulum in UT-1 cells and its disappearance in response to cholesterol
    • Anderson, R.G., Orci, L., Brown, M.S., Garcia-Segura, L.M., and Goldstein, J.L. (1983). Ultrastructural analysis of crystalloid endoplasmic reticulum in UT-1 cells and its disappearance in response to cholesterol. J. Cell Sci. 63, 1-20.
    • (1983) J. Cell Sci. , vol.63 , pp. 1-20
    • Anderson, R.G.1    Orci, L.2    Brown, M.S.3    Garcia-Segura, L.M.4    Goldstein, J.L.5
  • 3
    • 0023506415 scopus 로고
    • Identifying mutations in duplicated functions in Saccharomyces cerevisiae: Recessive mutations in HMG-CoA reductase genes
    • Basson, M.E., Moore, R.L., O'Rear, J., and Rine, J. (1987). Identifying mutations in duplicated functions in Saccharomyces cerevisiae: recessive mutations in HMG-CoA reductase genes. Genetics 117, 645-655.
    • (1987) Genetics , vol.117 , pp. 645-655
    • Basson, M.E.1    Moore, R.L.2    O'Rear, J.3    Rine, J.4
  • 4
    • 0023779728 scopus 로고
    • Structural and functional conservation between yeast and human 3-hydroxy-3-methylglutaryl CoA reductases, the rate-limiting enzyme of sterol biosynthesis
    • Basson, M.E., Thorsness, M., Finer-Moore, J., Stroud, R.M, and Rine, J. (1988). Structural and functional conservation between yeast and human 3-hydroxy-3-methylglutaryl CoA reductases, the rate-limiting enzyme of sterol biosynthesis. Mol. Cell. Biol. 8, 3797-3808.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 3797-3808
    • Basson, M.E.1    Thorsness, M.2    Finer-Moore, J.3    Stroud, R.M.4    Rine, J.5
  • 5
    • 1442283623 scopus 로고
    • Saccharomyces cerevisiae contains two functional genes encoding 3-hydroxy-3-methylglutaryl-CoA reductase
    • Basson, M.E., Thorsness, M., and Rine, J. (1986). Saccharomyces cerevisiae contains two functional genes encoding 3-hydroxy-3-methylglutaryl-CoA reductase. Proc. Natl. Acad. Sci. USA 83, 5563-5567.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 5563-5567
    • Basson, M.E.1    Thorsness, M.2    Rine, J.3
  • 6
    • 0024359563 scopus 로고
    • Cloning, sequencing, and overexpression of mvaA, which encodes Pseudomonas mevalonii 3-hydroxy-3-methylglutaryl CoA reductase
    • Beach, M.J., and Rodwell, V.W. (1989). Cloning, sequencing, and overexpression of mvaA, which encodes Pseudomonas mevalonii 3-hydroxy-3-methylglutaryl CoA reductase. J. Bacteriol. 171, 2994-3001.
    • (1989) J. Bacteriol. , vol.171 , pp. 2994-3001
    • Beach, M.J.1    Rodwell, V.W.2
  • 7
    • 0030029174 scopus 로고    scopus 로고
    • 3-Hydroxy-3-methylglutaryl-CoA reductase from Haloferax volcanii: Purification, characterization, and expression in Escherichia coli
    • Bischoff, K.M., and Rodwell, V.W. (1996). 3-Hydroxy-3-methylglutaryl-CoA reductase from Haloferax volcanii: purification, characterization, and expression in Escherichia coli. J. Bacteriol. 178, 19-23.
    • (1996) J. Bacteriol. , vol.178 , pp. 19-23
    • Bischoff, K.M.1    Rodwell, V.W.2
  • 8
    • 0031009135 scopus 로고    scopus 로고
    • 3-Hydroxy-3-methylglutaryl CoA reductase of Sulfolobus solfataricus: DNA sequence, phylogeny, expression in Escherichia coli of the hmgA gene, and purification and kinetic characterization of the gene product
    • Bochar, D.A., Brown, J.R., Doolittle, W.F., Klenk, H.P., Lam, W., Schenk, M.E., Stauffacher, C.V., and Rodwell, V.W. (1997). 3-Hydroxy-3-methylglutaryl CoA reductase of Sulfolobus solfataricus: DNA sequence, phylogeny, expression in Escherichia coli of the hmgA gene, and purification and kinetic characterization of the gene product. J. Bacteriol. 179, 3632-3638.
    • (1997) J. Bacteriol. , vol.179 , pp. 3632-3638
    • Bochar, D.A.1    Brown, J.R.2    Doolittle, W.F.3    Klenk, H.P.4    Lam, W.5    Schenk, M.E.6    Stauffacher, C.V.7    Rodwell, V.W.8
  • 9
    • 0029393978 scopus 로고
    • Green fluorescent protein
    • Chalfie, M. (1995). Green fluorescent protein. Photochem. Photobiol. 62, 651-656.
    • (1995) Photochem. Photobiol. , vol.62 , pp. 651-656
    • Chalfie, M.1
  • 10
    • 23444431611 scopus 로고
    • Green fluorescent protein as a marker for gene expression
    • Chalfie, M., Tu, Y., Euskirchen, G., Ward, W.W., and Prasher, D.C. (1994). Green fluorescent protein as a marker for gene expression. Science 263, 802-805.
    • (1994) Science , vol.263 , pp. 802-805
    • Chalfie, M.1    Tu, Y.2    Euskirchen, G.3    Ward, W.W.4    Prasher, D.C.5
  • 11
    • 0033546303 scopus 로고    scopus 로고
    • Oligomerization state influences the degradation rate of 3-hydroxy-3-methylglutaryl-CoA reductase
    • Cheng, H.H., Xu, L., Kumagai, H., and Simoni, R.D. (1999). Oligomerization state influences the degradation rate of 3-hydroxy-3-methylglutaryl-CoA reductase. J. Biol. Chem. 274, 17171-17178.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17171-17178
    • Cheng, H.H.1    Xu, L.2    Kumagai, H.3    Simoni, R.D.4
  • 12
    • 0141646834 scopus 로고
    • Appearance of crystalloid endoplasmic reticulum in compactin-resistant Chinese hamster cells with a 500-fold elevation in 3-hydroxy-3-methylglutaryl CoA reductase
    • Chin, D.J., Luskey, K.L., Anderson, R.G.W., Faust, J.R., Goldstein, J.L., and Brown, M.S. (1982). Appearance of crystalloid endoplasmic reticulum in compactin-resistant Chinese hamster cells with a 500-fold elevation in 3-hydroxy-3-methylglutaryl CoA reductase. Proc. Natl. Acad. Sci. USA 79, 1185-1189.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 1185-1189
    • Chin, D.J.1    Luskey, K.L.2    Anderson, R.G.W.3    Faust, J.R.4    Goldstein, J.L.5    Brown, M.S.6
  • 13
    • 0026742974 scopus 로고
    • The role of the membrane domain in the regulated degradation of 3-hydroxy-3-methylglutaryl CoA reductase
    • Chun, K.T., and Simoni, R.D. (1992). The role of the membrane domain in the regulated degradation of 3-hydroxy-3-methylglutaryl CoA reductase. J. Biol. Chem. 267, 4236-4246.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4236-4246
    • Chun, K.T.1    Simoni, R.D.2
  • 14
    • 0026683310 scopus 로고
    • Identification of the catalytically important histidine of 3-hydroxy-3-methylglutaryl-CoA reductase
    • Darnay, B.G., Y. Wang, and V.W. Rodwell. (1992). Identification of the catalytically important histidine of 3-hydroxy-3-methylglutaryl-CoA reductase. J. Biol. Chem. 267, 15064-15070.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15064-15070
    • Darnay, B.G.1    Wang, Y.2    Rodwell, V.W.3
  • 15
    • 0032907102 scopus 로고    scopus 로고
    • Integrins and signal transduction
    • Dedhar, S. (1999). Integrins and signal transduction. Curr. Opin. Hematol. 6, 37-43.
    • (1999) Curr. Opin. Hematol. , vol.6 , pp. 37-43
    • Dedhar, S.1
  • 16
    • 0029919182 scopus 로고    scopus 로고
    • The N-terminal domain of tomato 3-hydroxy-3-methylglutaryl-CoA reductases. Sequence, microsomal targeting, and glycosylation
    • Denbow, C.J., Lang, S., and Cramer, C.L. (1996). The N-terminal domain of tomato 3-hydroxy-3-methylglutaryl-CoA reductases. Sequence, microsomal targeting, and glycosylation. J. Biol. Chem. 271, 9710-9715.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9710-9715
    • Denbow, C.J.1    Lang, S.2    Cramer, C.L.3
  • 17
    • 0023374628 scopus 로고
    • Fatty acylation is important but not essential for Saccharomyces cerevisiae RAS function
    • Deschenes, R.J., and Broach, J.R. (1987). Fatty acylation is important but not essential for Saccharomyces cerevisiae RAS function. Mol. Cell. Biol. 7, 2344-2351.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2344-2351
    • Deschenes, R.J.1    Broach, J.R.2
  • 18
    • 0030772492 scopus 로고    scopus 로고
    • Effects of overproduction of the catalytic domain of 3-hydroxy-3-methylglutaryl CoA reductase on squalene synthesis in Saccharomyces cerevisiae
    • Donald, K.A., Hampton, R.Y., and Fritz, I.B. (1997). Effects of overproduction of the catalytic domain of 3-hydroxy-3-methylglutaryl CoA reductase on squalene synthesis in Saccharomyces cerevisiae. Appl. Environ. Microbiol. 63, 3341-3344.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 3341-3344
    • Donald, K.A.1    Hampton, R.Y.2    Fritz, I.B.3
  • 19
    • 0030023247 scopus 로고    scopus 로고
    • Determining divergence times of the major kingdoms of living organisms with a protein clock
    • Doolittle, R.F., Feng, D.F., Tsang, S., Cho, G., and Little, E. (1996). Determining divergence times of the major kingdoms of living organisms with a protein clock. Science 271, 470-477.
    • (1996) Science , vol.271 , pp. 470-477
    • Doolittle, R.F.1    Feng, D.F.2    Tsang, S.3    Cho, G.4    Little, E.5
  • 20
    • 0022359706 scopus 로고
    • Functional size of rat hepatic 3-hydroxy-3-methylglutaryl CoA reductase as determined by radiation inactivation
    • Edwards, P.A., Kempner, E.S., Lan, S.-F., and Erickson, S.K. (1985). Functional size of rat hepatic 3-hydroxy-3-methylglutaryl CoA reductase as determined by radiation inactivation. J. Biol. Chem. 260, 10278-10282.
    • (1985) J. Biol. Chem. , vol.260 , pp. 10278-10282
    • Edwards, P.A.1    Kempner, E.S.2    Lan, S.-F.3    Erickson, S.K.4
  • 21
    • 0003945763 scopus 로고
    • Philadelphia: W.B. Saunders
    • Fawcett, D.W. (1981). The Cell, Philadelphia: W.B. Saunders, 301-368.
    • (1981) The Cell , pp. 301-368
    • Fawcett, D.W.1
  • 22
    • 0030696044 scopus 로고    scopus 로고
    • Determining divergence times with a protein clock: Update and reevaluation
    • Feng, D.F., Cho, G., and Doolittle, R.F. (1997). Determining divergence times with a protein clock: update and reevaluation [see comments]. Proc. Natl. Acad. Sci. USA 94, 13028-13033.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13028-13033
    • Feng, D.F.1    Cho, G.2    Doolittle, R.F.3
  • 23
    • 0014028194 scopus 로고
    • Colinearity of beta-galactosidase with its gene by immunological detection of incomplete polypeptide chains
    • Fowler, A.V., and Zabin, I. (1966). Colinearity of beta-galactosidase with its gene by immunological detection of incomplete polypeptide chains. Science 154, 1027-1029.
    • (1966) Science , vol.154 , pp. 1027-1029
    • Fowler, A.V.1    Zabin, I.2
  • 24
    • 0014413526 scopus 로고
    • Beta-galactosidase: Immunological studies of nonsense, missense and deletion mutants
    • Fowler, A.V., and Zabin, I. (1968). Beta-galactosidase: immunological studies of nonsense, missense and deletion mutants. J. Mol. Biol. 33, 35-47.
    • (1968) J. Mol. Biol. , vol.33 , pp. 35-47
    • Fowler, A.V.1    Zabin, I.2
  • 25
    • 0021100436 scopus 로고
    • Purification, structure, and properties of hybrid beta-galactosidase proteins
    • Fowler, A.V., and Zabin, I. (1983). Purification, structure, and properties of hybrid beta-galactosidase proteins. J. Biol. Chem. 258, 14354-14358.
    • (1983) J. Biol. Chem. , vol.258 , pp. 14354-14358
    • Fowler, A.V.1    Zabin, I.2
  • 26
    • 0027955168 scopus 로고
    • The active site of hamster 3-hydroxy-3-methylglutaryl-CoA reductase resides at the subunit interface and incorporates catalytically essential acidic residues from separate polypeptides
    • Frimpong, K., and Rodwell, V.W. (1994). The active site of hamster 3-hydroxy-3-methylglutaryl-CoA reductase resides at the subunit interface and incorporates catalytically essential acidic residues from separate polypeptides. J. Biol. Chem. 269, 1217-1221.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1217-1221
    • Frimpong, K.1    Rodwell, V.W.2
  • 27
    • 0031713885 scopus 로고    scopus 로고
    • Sequence determinants for regulated degradation of yeast 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein
    • erratum [1999]. 10[3]
    • Gardner, R., Cronin, S., Leader, B., Rine, J., Hampton, R., and Leder, B. (1998). Sequence determinants for regulated degradation of yeast 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein. Mol Biol Cell 9, 2611-2626 (erratum [1999]. 10[3]).
    • (1998) Mol Biol Cell , vol.9 , pp. 2611-2626
    • Gardner, R.1    Cronin, S.2    Leader, B.3    Rine, J.4    Hampton, R.5    Leder, B.6
  • 28
    • 0030859541 scopus 로고    scopus 로고
    • Agonists induce conformational changes in transmembrane domains III and VI of the beta2 adrenoceptor
    • Gether, U., Lin, S., Ghanouni, P., Ballesteros, J.A., Weinstein, H., and Kobilka, B.K. (1997). Agonists induce conformational changes in transmembrane domains III and VI of the beta2 adrenoceptor. EMBO J. 16, 6737-6747.
    • (1997) EMBO J. , vol.16 , pp. 6737-6747
    • Gether, U.1    Lin, S.2    Ghanouni, P.3    Ballesteros, J.A.4    Weinstein, H.5    Kobilka, B.K.6
  • 29
    • 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., and Brown, M.S. (1985). Membrane-bound domain of HMG CoA reductase is required for sterol-enhanced degradation of the enzyme. Cell 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
  • 31
  • 32
    • 0009355836 scopus 로고
    • Fusion of Escherichia coli lacZ to the cytochrome c gene of Saccharomyces cerevisiae
    • Guarente, L., and Ptashne, M. (1981). Fusion of Escherichia coli lacZ to the cytochrome c gene of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 78, 2199-2203.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 2199-2203
    • Guarente, L.1    Ptashne, M.2
  • 33
    • 0030069686 scopus 로고    scopus 로고
    • In vivo examination of membrane protein localization and degradation with GFP
    • Hampton, R.Y., Koning, A., Wright, R., and Rine, J. (1996). In vivo examination of membrane protein localization and degradation with GFP. Proc. Natl. Acad. Sci. USA 93, 828-833.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 828-833
    • Hampton, R.Y.1    Koning, A.2    Wright, R.3    Rine, J.4
  • 34
    • 0028213166 scopus 로고
    • Regulated degradation of HMG-CoA reductase, an integral membrane protein of the endoplasmic reticulum, in yeast
    • Hampton, R.Y., and Rine, J. (1994). Regulated degradation of HMG-CoA reductase, an integral membrane protein of the endoplasmic reticulum, in yeast. J. Cell Biol. 125, 299-312.
    • (1994) J. Cell Biol. , vol.125 , pp. 299-312
    • Hampton, R.Y.1    Rine, J.2
  • 35
    • 0029048813 scopus 로고
    • The conserved membrane-proximal region of an integrin cytoplasmic domain specifies ligand binding affinity
    • Hughes, P.E., O'Toole, T.E., Ylanne, J., Shattil, S.J., and Ginsberg, M.H. (1995). The conserved membrane-proximal region of an integrin cytoplasmic domain specifies ligand binding affinity. J. Biol. Chem. 270, 12411-12417.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12411-12417
    • Hughes, P.E.1    O'Toole, T.E.2    Ylanne, J.3    Shattil, S.J.4    Ginsberg, M.H.5
  • 36
    • 0023202281 scopus 로고
    • Partial deletion of membrane-bound domain of 3-hydroxy-3-methylglutaryl CoA reductase eliminates sterol-enhanced degradation and prevents formation of crystalloid endoplasmic reticulum
    • Jingami, H., Brown, M.S., Goldstein, J.L., Anderson, R.G., and Luskey, K.L. (1987). Partial deletion of membrane-bound domain of 3-hydroxy-3-methylglutaryl CoA reductase eliminates sterol-enhanced degradation and prevents formation of crystalloid endoplasmic reticulum. J. Cell Biol. 104, 1693-1704.
    • (1987) J. Cell Biol. , vol.104 , pp. 1693-1704
    • Jingami, H.1    Brown, M.S.2    Goldstein, J.L.3    Anderson, R.G.4    Luskey, K.L.5
  • 37
    • 0023664675 scopus 로고
    • Purified crystalloid endoplasmic reticulum from UT-1 cells contains multiple proteins in addition to 3-hydroxy-3-methylglutaryl CoA reductase
    • Kochevar, D., and Anderson, R.G.W. (1987). Purified crystalloid endoplasmic reticulum from UT-1 cells contains multiple proteins in addition to 3-hydroxy-3-methylglutaryl CoA reductase. J. Biol. Chem. 262, 10321-10326.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10321-10326
    • Kochevar, D.1    Anderson, R.G.W.2
  • 39
    • 0029926584 scopus 로고    scopus 로고
    • Different subcellular localization of Saccharomyces cerevisiae HMG-CoA reductase isozymes at elevated levels corresponds to distinct endoplasmic reticulum membrane proliferations
    • Koning, A.J., Roberts, C.J., and Wright, R.L. (1996). Different subcellular localization of Saccharomyces cerevisiae HMG-CoA reductase isozymes at elevated levels corresponds to distinct endoplasmic reticulum membrane proliferations. Mol. Biol. Cell 7, 769-789.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 769-789
    • Koning, A.J.1    Roberts, C.J.2    Wright, R.L.3
  • 40
    • 0029045589 scopus 로고
    • Molecular dissection of the role of the membrane domain in the regulated degradation of 3-hydroxy-3-methylglutaryl CoA reductase
    • Kumagai, H., Chun, K.T., and Simoni, R.D. (1995). Molecular dissection of the role of the membrane domain in the regulated degradation of 3-hydroxy-3-methylglutaryl CoA reductase. J. Biol. Chem. 270, 19107-19113.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19107-19113
    • Kumagai, H.1    Chun, K.T.2    Simoni, R.D.3
  • 41
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 42
  • 43
    • 0029066497 scopus 로고
    • Crystal structure of Pseudomonas mevalonii HMG-CoA reductase at 3.0 angstrom resolution
    • Lawrence, C.M., Rodwell, V.W., and Stauffacher, C.V. (1995). Crystal structure of Pseudomonas mevalonii HMG-CoA reductase at 3.0 angstrom resolution. Science 268, 1758-1762.
    • (1995) Science , vol.268 , pp. 1758-1762
    • Lawrence, C.M.1    Rodwell, V.W.2    Stauffacher, C.V.3
  • 44
    • 0033617417 scopus 로고    scopus 로고
    • Bidirectional transmembrane modulation of integrin alphaIIbbeta3 conformations
    • Leisner, T.M., Wencel-Drake, J.D., Wang, W., and Lam, S.C. (1999). Bidirectional transmembrane modulation of integrin alphaIIbbeta3 conformations. J. Biol. Chem. 274, 12945-12949.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12945-12949
    • Leisner, T.M.1    Wencel-Drake, J.D.2    Wang, W.3    Lam, S.C.4
  • 45
    • 0021913335 scopus 로고
    • Domain structure of 3-hydroxy-3-methylglutaryl CoA 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 CoA 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
  • 46
    • 0029839311 scopus 로고    scopus 로고
    • Molecular, functional, and evolutionary characterization of the gene encoding HMG-CoA reductase in the fission yeast, Schizosaccharomyces pombe
    • Lum, P.Y., Edwards, S., and Wright, R. (1996). Molecular, functional, and evolutionary characterization of the gene encoding HMG-CoA reductase in the fission yeast, Schizosaccharomyces pombe. Yeast 12, 1107-1124.
    • (1996) Yeast , vol.12 , pp. 1107-1124
    • Lum, P.Y.1    Edwards, S.2    Wright, R.3
  • 47
    • 0029165402 scopus 로고
    • Degradation of HMG CoA reductase-induced membranes in the fission yeast. Schizosaccharomyces pombe
    • Lum, P.Y., and Wright, R. (1995). Degradation of HMG CoA reductase-induced membranes in the fission yeast. Schizosaccharomyces pombe. J. Cell Biol. 131, 81-94.
    • (1995) J. Cell Biol. , vol.131 , pp. 81-94
    • Lum, P.Y.1    Wright, R.2
  • 48
    • 0028068939 scopus 로고
    • Microsomal aldehyde dehydrogenase is localized to the endoplasmic reticulum via its carboxyl-terminal 35 amino acids
    • Masaki, R., Yamamoto, A., and Tashiro, Y. (1994). Microsomal aldehyde dehydrogenase is localized to the endoplasmic reticulum via its carboxyl-terminal 35 amino acids. J. Cell Biol. 126, 1407-1420.
    • (1994) J. Cell Biol. , vol.126 , pp. 1407-1420
    • Masaki, R.1    Yamamoto, A.2    Tashiro, Y.3
  • 49
    • 0029975529 scopus 로고    scopus 로고
    • Membrane topology and retention of microsomal aldehyde dehydrogenase in the endoplasmic reticulum
    • Masaki, R., Yamamoto, A., and Tashiro, Y. (1996). Membrane topology and retention of microsomal aldehyde dehydrogenase in the endoplasmic reticulum. J. Biol. Chem. 271, 16939-16944.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16939-16944
    • Masaki, R.1    Yamamoto, A.2    Tashiro, Y.3
  • 50
    • 0031876599 scopus 로고    scopus 로고
    • The PBN1 gene of Saccharomyces cerevisiae: An essential gene that is required for the posttranslational processing of the protease B precursor
    • Naik, R.R., and Jones, E.W. (1998). The PBN1 gene of Saccharomyces cerevisiae: an essential gene that is required for the posttranslational processing of the protease B precursor. Genetics 149, 1277-1292.
    • (1998) Genetics , vol.149 , pp. 1277-1292
    • Naik, R.R.1    Jones, E.W.2
  • 51
    • 0028073895 scopus 로고
    • Inhibition of endoplasmic reticulum (ER)-to-Golgi transport induces relocalization of binding protein (BiP) within the ER to form the BiP bodies
    • Nishikawa, S., Hirata, A., and Nakano, A. (1994). Inhibition of endoplasmic reticulum (ER)-to-Golgi transport induces relocalization of binding protein (BiP) within the ER to form the BiP bodies. Mol. Biol. Cell 5, 1129-1143.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 1129-1143
    • Nishikawa, S.1    Hirata, A.2    Nakano, A.3
  • 52
    • 0026673416 scopus 로고
    • The intracellular targeting and membrane topology of 3-hydroxy-3-methylglutaryl-CoA reductase
    • Olender, E.H., and Simon, R.D. (1992). The intracellular targeting and membrane topology of 3-hydroxy-3-methylglutaryl-CoA reductase. J. Biol. Chem. 267, 4223-4235.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4223-4235
    • Olender, E.H.1    Simon, R.D.2
  • 53
    • 0021417623 scopus 로고
    • Increase in membrane cholesterol: A possible trigger for degradation of HMG CoA reductase and crystalloid endoplasmic reticulum in UT-1 cells
    • Orci, L., Brown, M.S., Goldstein, J.L., Garcia-Segura, L.M., and Anderson, R.G. (1984). Increase in membrane cholesterol: a possible trigger for degradation of HMG CoA reductase and crystalloid endoplasmic reticulum in UT-1 cells. Cell 36, 835-845.
    • (1984) Cell , vol.36 , pp. 835-845
    • Orci, L.1    Brown, M.S.2    Goldstein, J.L.3    Garcia-Segura, L.M.4    Anderson, R.G.5
  • 54
    • 0031899024 scopus 로고    scopus 로고
    • Related membrane domains in proteins of sterol sensing and cell signaling provide a glimpse of treasures still buried within the dynamic realm of intracellular metabolic regulation
    • Osborne, T.F., and Rosenfeld, J.M. (1998). Related membrane domains in proteins of sterol sensing and cell signaling provide a glimpse of treasures still buried within the dynamic realm of intracellular metabolic regulation. Curr. Opin. Lipidol. 9, 137-140.
    • (1998) Curr. Opin. Lipidol. , vol.9 , pp. 137-140
    • Osborne, T.F.1    Rosenfeld, J.M.2
  • 56
    • 0028864187 scopus 로고
    • Identification of the sequences in HMG-CoA reductase required for karmellae assembly
    • Parrish, M.L., Sengstag, C., Rine, J.D., and Wright, R.L. (1995). Identification of the sequences in HMG-CoA reductase required for karmellae assembly. Mol. Biol. Cell 6, 1535-1547.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1535-1547
    • Parrish, M.L.1    Sengstag, C.2    Rine, J.D.3    Wright, R.L.4
  • 57
    • 0022540905 scopus 로고
    • Biogenesis of the crystalloid endoplasmic reticulum in UT-1 cells: Evidence that newly formed endoplasmic reticulum emerges from the nuclear envelope
    • Pathak, R.K., Luskey, K.L., and Anderson, R.G. (1986). Biogenesis of the crystalloid endoplasmic reticulum in UT-1 cells: evidence that newly formed endoplasmic reticulum emerges from the nuclear envelope. J. Cell Biol. 102, 2158-2168.
    • (1986) J. Cell Biol. , vol.102 , pp. 2158-2168
    • Pathak, R.K.1    Luskey, K.L.2    Anderson, R.G.3
  • 58
    • 0029134629 scopus 로고
    • Using GFP to see the light
    • Prasher, D.C. (1995). Using GFP to see the light. Trends Genet. 11, 320-323.
    • (1995) Trends Genet. , vol.11 , pp. 320-323
    • Prasher, D.C.1
  • 59
    • 0026578325 scopus 로고
    • Primary structure of the Aequorea victoria green-fluorescent protein
    • Prasher, D.C., Eckenrode, V.K., Ward, W.W., Prendergast, F.G., and Cormier, M.J. (1992). Primary structure of the Aequorea victoria green-fluorescent protein. Gene 111, 229-233.
    • (1992) Gene , vol.111 , pp. 229-233
    • Prasher, D.C.1    Eckenrode, V.K.2    Ward, W.W.3    Prendergast, F.G.4    Cormier, M.J.5
  • 60
    • 0026335172 scopus 로고
    • Structure of the yeast endoplasmic reticulum: Localization of ER proteins using immunofluorescence and immunoelectron microscopy
    • Preuss, D., Mulholland, J., Kaiser, C.A., Orlean, P., Albright, C., Rose, M.D., Robbins, P.W., and Botstein, D. (1991). Structure of the yeast endoplasmic reticulum: localization of ER proteins using immunofluorescence and immunoelectron microscopy. Yeast 7, 891-911.
    • (1991) Yeast , vol.7 , pp. 891-911
    • Preuss, D.1    Mulholland, J.2    Kaiser, C.A.3    Orlean, P.4    Albright, C.5    Rose, M.D.6    Robbins, P.W.7    Botstein, D.8
  • 62
    • 0030945772 scopus 로고    scopus 로고
    • Genetic and biochemical analysis of the transmembrane domain of Arabidopsis 3-hydroxy-3-methylglutaryl CoA reductase
    • Re, E.B., Brugger, S., and Learned, M. (1997). Genetic and biochemical analysis of the transmembrane domain of Arabidopsis 3-hydroxy-3-methylglutaryl CoA reductase. J. Cell Biochem. 65, 443-459.
    • (1997) J. Cell Biochem. , vol.65 , pp. 443-459
    • Re, E.B.1    Brugger, S.2    Learned, M.3
  • 63
    • 0033548048 scopus 로고    scopus 로고
    • Erythropoietin receptor activation by a ligand-induced conformation change
    • Remy, I., Wilson, I.A., and Michnick, S.W. (1999). Erythropoietin receptor activation by a ligand-induced conformation change. Science 283, 990-993.
    • (1999) Science , vol.283 , pp. 990-993
    • Remy, I.1    Wilson, I.A.2    Michnick, S.W.3
  • 64
    • 52649114611 scopus 로고
    • The use of lead citrate at high pH as an electron-opaque stain in electron microscopy
    • Reynolds, E.S. (1963). The use of lead citrate at high pH as an electron-opaque stain in electron microscopy. J. Cell Biol. 17, 208-212.
    • (1963) J. Cell Biol. , vol.17 , pp. 208-212
    • Reynolds, E.S.1
  • 65
    • 0031171975 scopus 로고    scopus 로고
    • Active form of Pseudomonas mevalonii 3-hydroxy-3-methylglutaryl CoA reductase
    • Rogers, K.S., Rodwell, V.W., and Geiger, P. (1997). Active form of Pseudomonas mevalonii 3-hydroxy-3-methylglutaryl CoA reductase. Biochem. Mol. Med. 61, 114-120.
    • (1997) Biochem. Mol. Med. , vol.61 , pp. 114-120
    • Rogers, K.S.1    Rodwell, V.W.2    Geiger, P.3
  • 66
    • 0026072178 scopus 로고
    • Involvement of calcium in the mevalonate-accelerated degradation of 3-hydroxy-3-methylglutaryl-CoA reductase
    • Roitelman, J., Bar-Nun, S., Inoue, S., and Simoni, R.D. (1991). Involvement of calcium in the mevalonate-accelerated degradation of 3-hydroxy-3-methylglutaryl-CoA reductase. J. Biol. Chem. 266, 16085-16091.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16085-16091
    • Roitelman, J.1    Bar-Nun, S.2    Inoue, S.3    Simoni, R.D.4
  • 67
    • 0026720521 scopus 로고
    • Immunolgical 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, J.W.A., and Simoni, R.D. (1992). Immunolgical 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. 5, 959-973.
    • (1992) J. Cell Biol. , vol.5 , pp. 959-973
    • Roitelman, J.1    Olender, E.H.2    Bar-Nun, S.3    Dunn, J.W.A.4    Simoni, R.D.5
  • 68
    • 0024338964 scopus 로고
    • KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene
    • Rose, M.D., L.M. Mistra, and J.P. Vogel. (1989). KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene. Cell 57, 1211-1221.
    • (1989) Cell , vol.57 , pp. 1211-1221
    • Rose, M.D.1    Mistra, L.M.2    Vogel, J.P.3
  • 69
    • 0025883783 scopus 로고
    • Comparision of two cytochromes P-450 from Candida maltosa: Primary structures, substrate specificities and effects of their expression in Saccharomyces cerevisiae on the proliferation of the endoplasmic reticulum
    • Schunck, W., Vogel, F., Gross, B., Kargel, E., Mauersberger, S., Kopke, K., Gengnagel, C., and Muller, H. (1991). Comparision of two cytochromes P-450 from Candida maltosa: primary structures, substrate specificities and effects of their expression in Saccharomyces cerevisiae on the proliferation of the endoplasmic reticulum. Eur. J. Cell Biol. 55, 336-345.
    • (1991) Eur. J. Cell Biol. , vol.55 , pp. 336-345
    • Schunck, W.1    Vogel, F.2    Gross, B.3    Kargel, E.4    Mauersberger, S.5    Kopke, K.6    Gengnagel, C.7    Muller, H.8
  • 70
    • 0028797806 scopus 로고
    • Mutation in the lumenal part of the membrane domain of HMG-CoA reductase alters its regulated degradation
    • Sekler, M.S., and Simoni, R.D. (1995). Mutation in the lumenal part of the membrane domain of HMG-CoA reductase alters its regulated degradation. Biochem. Biophys. Res. Commun. 206, 186-193.
    • (1995) Biochem. Biophys. Res. Commun. , vol.206 , pp. 186-193
    • Sekler, M.S.1    Simoni, R.D.2
  • 71
    • 0025099013 scopus 로고
    • Genetic and biochemical evaluation of eukaryotic membrane protein topology: The polytopic structure of S. cerevisiae HMG-CoA reductase
    • Sengstag, C., Stirling, C., Schekman, R., and Rine, J. (1990). Genetic and biochemical evaluation of eukaryotic membrane protein topology: the polytopic structure of S. cerevisiae HMG-CoA reductase. Mol. Cell. Biol. 10, 672-680.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 672-680
    • Sengstag, C.1    Stirling, C.2    Schekman, R.3    Rine, J.4
  • 73
    • 0024669291 scopus 로고
    • A uniform set of multipurpose shuttle vectors and yeast host strains designed for efficient manipulation of DNA in S. cerevisiae
    • Sikorski, R.S., and Hieter, P. (1989). A uniform set of multipurpose shuttle vectors and yeast host strains designed for efficient manipulation of DNA in S. cerevisiae. Genetics 122, 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 74
    • 0024287649 scopus 로고
    • The membrane domain of 3-hydroxy-3-methylglutaryl CoA reductase confers endoplasmic reticulum localization and sterol-regulated degradation onto β-galactosidase
    • Skalnik, D.G., Narita, H., Kent, C., and Simoni, R.D. (1988). The membrane domain of 3-hydroxy-3-methylglutaryl CoA reductase confers endoplasmic reticulum localization and sterol-regulated degradation onto β-galactosidase. J. Biol. Chem. 263, 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
  • 75
    • 0014444144 scopus 로고
    • A low-viscosity epoxy resin embedding medium for electron microscopy
    • Spurr, A.R. (1969). A low-viscosity epoxy resin embedding medium for electron microscopy. J. UItrastruct. Res. 26, 31-43.
    • (1969) J. Uitrastruct. Res. , vol.26 , pp. 31-43
    • Spurr, A.R.1
  • 76
    • 0033595021 scopus 로고    scopus 로고
    • Substrate-induced closure of the flap domain in the ternary complex structures provides insights into the mechanism of catalysis by 3-hydroxy-3-methylglutaryl-CoA reductase
    • Tabernero, L., Bochar, D.A., Rodwell, V.W., and Stauffacher, C.V. (1999). Substrate-induced closure of the flap domain in the ternary complex structures provides insights into the mechanism of catalysis by 3-hydroxy-3-methylglutaryl-CoA reductase. Proc. Natl. Acad. Sci. USA 96, 7167-7171.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7167-7171
    • Tabernero, L.1    Bochar, D.A.2    Rodwell, V.W.3    Stauffacher, C.V.4
  • 77
    • 0033028107 scopus 로고    scopus 로고
    • Purification, characterization, and cloning of a eubacterial 3-hydroxy-3-methylglutaryl CoA reductase, a key enzyme involved in biosynthesis of terpenoids
    • Takahashi, S., Kuzuyama, T., and Seto, H. (1999). Purification, characterization, and cloning of a eubacterial 3-hydroxy-3-methylglutaryl CoA reductase, a key enzyme involved in biosynthesis of terpenoids. J. Bacteriol. 181, 1256-1263.
    • (1999) J. Bacteriol. , vol.181 , pp. 1256-1263
    • Takahashi, S.1    Kuzuyama, T.2    Seto, H.3
  • 78
    • 0026800860 scopus 로고
    • Degradation of a nuclear-localized protein in mammalian COS cells, using Escherichia coli beta-galactosidase as a model protein
    • Tsuneoka, M., and Mekada, E. (1992). Degradation of a nuclear-localized protein in mammalian COS cells, using Escherichia coli beta-galactosidase as a model protein. J. Biol. Chem. 267, 9107-9111.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9107-9111
    • Tsuneoka, M.1    Mekada, E.2
  • 80
    • 0029054827 scopus 로고
    • Functional characterization of the 180-kD ribosome receptor in vivo
    • Wanker, E.E., Sun, Y., Savitz, A.J., and Meyer, D.I. (1995). Functional characterization of the 180-kD ribosome receptor in vivo. J. Cell Biol. 130, 29-39.
    • (1995) J. Cell Biol. , vol.130 , pp. 29-39
    • Wanker, E.E.1    Sun, Y.2    Savitz, A.J.3    Meyer, D.I.4
  • 82
    • 0023788653 scopus 로고
    • Increased amounts of HMG-CoA reductase induce "karmellae": A proliferation of stacked membrane pairs surrounding the yeast nucleus
    • Wright, R., Basson, M., D'Ari, L., and Rine, J. (1988). Increased amounts of HMG-CoA reductase induce "karmellae": a proliferation of stacked membrane pairs surrounding the yeast nucleus. J. Cell Biol. 107, 101-114.
    • (1988) J. Cell Biol. , vol.107 , pp. 101-114
    • Wright, R.1    Basson, M.2    D'Ari, L.3    Rine, J.4
  • 83
    • 0024388570 scopus 로고
    • Transmission electron microscopy and immunocytochemical studies of yeast: Analysis of HMG-CoA reductase overproduction by electron microscopy
    • Wright, R., and Rine, J. (1989). Transmission electron microscopy and immunocytochemical studies of yeast: analysis of HMG-CoA reductase overproduction by electron microscopy. Methods Cell Biol. 31, 473-512.
    • (1989) Methods Cell Biol. , vol.31 , pp. 473-512
    • Wright, R.1    Rine, J.2
  • 84
    • 0029993184 scopus 로고    scopus 로고
    • Formation of crystalloid endoplasmic reticulum in COS cells upon overexpression of microsomal aldehyde dehydrogenase by cDNA transfection
    • Yamamoto, A., Masaki, R., and Tashiro, Y. (1996). Formation of crystalloid endoplasmic reticulum in COS cells upon overexpression of microsomal aldehyde dehydrogenase by cDNA transfection. J. Cell Sci. 109, 1727-1738.
    • (1996) J. Cell Sci. , vol.109 , pp. 1727-1738
    • Yamamoto, A.1    Masaki, R.2    Tashiro, Y.3
  • 85
    • 0029044647 scopus 로고
    • Ultrastructural, immunocytochemical and stereological investigation of hepatocytes in a patient with the mutation of the omithine transcarbamylase gene
    • Zimmer, K.P., Matsuda, I., Matsuura, T., Mori, M., Colombo, J.P., Fahimi, H.D., Koch, H.G., Ullrich, K., and Harms, E. (1995). Ultrastructural, immunocytochemical and stereological investigation of hepatocytes in a patient with the mutation of the omithine transcarbamylase gene. Eur. J. Cell. Biol. 67, 73-83.
    • (1995) Eur. J. Cell. Biol. , vol.67 , pp. 73-83
    • Zimmer, K.P.1    Matsuda, I.2    Matsuura, T.3    Mori, M.4    Colombo, J.P.5    Fahimi, H.D.6    Koch, H.G.7    Ullrich, K.8    Harms, E.9


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