메뉴 건너뛰기




Volumn 199, Issue , 2016, Pages 170-178

Cholesterol homeostasis: How do cells sense sterol excess?

Author keywords

Cholesterol; Cholesterol sensing; Homeostasis; Membranes; Oxysterols

Indexed keywords

CHOLESTEROL; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; LIVER X RECEPTOR; OXYSTEROL; STEROL REGULATORY ELEMENT BINDING PROTEIN;

EID: 84962164803     PISSN: 00093084     EISSN: 18732941     Source Type: Journal    
DOI: 10.1016/j.chemphyslip.2016.02.011     Document Type: Article
Times cited : (50)

References (76)
  • 1
    • 0141591549 scopus 로고    scopus 로고
    • Cholesterol-induced conformational change in SCAP enhanced by Insig proteins and mimicked by cationic amphiphiles
    • Adams, C.M., Goldstein, J.L., Brown, M.S., Cholesterol-induced conformational change in SCAP enhanced by Insig proteins and mimicked by cationic amphiphiles. Proc. Natl. Acad. Sci. U. S. A. 100 (2003), 10647–10652, 10.1073/pnas.1534833100.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 10647-10652
    • Adams, C.M.1    Goldstein, J.L.2    Brown, M.S.3
  • 2
    • 84860158205 scopus 로고    scopus 로고
    • Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor
    • Baier, C.J., Fantini, J., Barrantes, F.J., Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor. Sci. Rep., 1, 2011, 69, 10.1038/srep00069.
    • (2011) Sci. Rep. , vol.1 , pp. 69
    • Baier, C.J.1    Fantini, J.2    Barrantes, F.J.3
  • 4
    • 33748325741 scopus 로고    scopus 로고
    • Erlin-1 and erlin-2 are novel members of the prohibitin family of proteins that define lipid-raft-like domains of the ER
    • Browman, D.T., Resek, M.E., Zajchowski, L.D., Robbins, S.M., Erlin-1 and erlin-2 are novel members of the prohibitin family of proteins that define lipid-raft-like domains of the ER. J. Cell Sci. 119 (2006), 3149–3160, 10.1242/jcs.03060.
    • (2006) J. Cell Sci. , vol.119 , pp. 3149-3160
    • Browman, D.T.1    Resek, M.E.2    Zajchowski, L.D.3    Robbins, S.M.4
  • 5
    • 0022549920 scopus 로고
    • A receptor-mediated pathway for cholesterol homeostasis
    • Brown, M.S., Goldstein, J.L., A receptor-mediated pathway for cholesterol homeostasis. Science 232 (1986), 34–47.
    • (1986) Science , vol.232 , pp. 34-47
    • Brown, M.S.1    Goldstein, J.L.2
  • 6
    • 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
  • 7
    • 0036671360 scopus 로고    scopus 로고
    • Cholesterol addition to ER membranes alters conformation of SCAP: the SREBP escort protein that regulates cholesterol metabolism
    • Brown, A.J., Sun, L., Feramisco, J.D., Brown, M.S., Goldstein, J.L., Cholesterol addition to ER membranes alters conformation of SCAP: the SREBP escort protein that regulates cholesterol metabolism. Mol. Cell 10 (2002), 237–245.
    • (2002) Mol. Cell , vol.10 , pp. 237-245
    • Brown, A.J.1    Sun, L.2    Feramisco, J.D.3    Brown, M.S.4    Goldstein, J.L.5
  • 9
    • 85006314789 scopus 로고    scopus 로고
    • Three pools of plasma membrane cholesterol and their relation to cholesterol homeostasis
    • Das, A., Brown, M.S., Anderson, D.D., Goldstein, J.L., Radhakrishnan, A., Three pools of plasma membrane cholesterol and their relation to cholesterol homeostasis. Elife, 2014, 10.7554/eLife.02882.
    • (2014) Elife
    • Das, A.1    Brown, M.S.2    Anderson, D.D.3    Goldstein, J.L.4    Radhakrishnan, A.5
  • 11
    • 0037012907 scopus 로고    scopus 로고
    • Regulation of SREBP processing and membrane lipid production by phospholipids in Drosophila
    • Dobrosotskaya, I.Y., Seegmiller, A.C., Brown, M.S., Goldstein, J.L., Rawson, R.B., Regulation of SREBP processing and membrane lipid production by phospholipids in Drosophila. Science 296 (2002), 879–883, 10.1126/science.1071124.
    • (2002) Science , vol.296 , pp. 879-883
    • Dobrosotskaya, I.Y.1    Seegmiller, A.C.2    Brown, M.S.3    Goldstein, J.L.4    Rawson, R.B.5
  • 12
    • 67349185295 scopus 로고    scopus 로고
    • Sterols and membrane dynamics
    • Dufourc, E.J., Sterols and membrane dynamics. J. Chem. Biol. 1 (2008), 63–77, 10.1007/s12154-008-0010-6.
    • (2008) J. Chem. Biol. , vol.1 , pp. 63-77
    • Dufourc, E.J.1
  • 13
    • 33744512299 scopus 로고    scopus 로고
    • Cholesterol and the interaction of proteins with membrane domains
    • Epand, R.M., Cholesterol and the interaction of proteins with membrane domains. Prog. Lipid Res. 45 (2006), 279–294, 10.1016/j.plipres.2006.02.001.
    • (2006) Prog. Lipid Res. , vol.45 , pp. 279-294
    • Epand, R.M.1
  • 14
    • 71549116093 scopus 로고    scopus 로고
    • Sphingolipid/cholesterol regulation of neurotransmitter receptor conformation and function
    • Fantini, J., Barrantes, F.J., Sphingolipid/cholesterol regulation of neurotransmitter receptor conformation and function. Biochim. Biophys. Acta, 2009, 2345–2361, 10.1016/j.bbamem.2009.08.016.
    • (2009) Biochim. Biophys. Acta , pp. 2345-2361
    • Fantini, J.1    Barrantes, F.J.2
  • 15
    • 84883556425 scopus 로고    scopus 로고
    • How cholesterol interacts with membrane proteins: an exploration of cholesterol-binding sites including CRAC, CARC, and tilted domains
    • Fantini, J., Barrantes, F.J., How cholesterol interacts with membrane proteins: an exploration of cholesterol-binding sites including CRAC, CARC, and tilted domains. Front. Physiol., 2013, 10.3389/fphys.2013.00031.
    • (2013) Front. Physiol.
    • Fantini, J.1    Barrantes, F.J.2
  • 16
    • 1542379024 scopus 로고    scopus 로고
    • Membrane topology of human insig-1, a protein regulator of lipid synthesis
    • Feramisco, J.D., Goldstein, J.L., Brown, M.S., Membrane topology of human insig-1, a protein regulator of lipid synthesis. J. Biol. Chem. 279 (2004), 8487–8496, 10.1074/jbc.M312623200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 8487-8496
    • Feramisco, J.D.1    Goldstein, J.L.2    Brown, M.S.3
  • 18
    • 53149118574 scopus 로고    scopus 로고
    • Sterol regulators of cholesterol homeostasis and beyond: the oxysterol hypothesis revisited and revised
    • Gill, S., Chow, R., Brown, A.J., Sterol regulators of cholesterol homeostasis and beyond: the oxysterol hypothesis revisited and revised. Prog. Lipid Res. 47 (2008), 391–404, 10.1016/j.plipres.2008.04.002.
    • (2008) Prog. Lipid Res. , vol.47 , pp. 391-404
    • Gill, S.1    Chow, R.2    Brown, A.J.3
  • 19
    • 79952174597 scopus 로고    scopus 로고
    • Cholesterol-dependent degradation of squalene monooxygenase, a control point in cholesterol synthesis beyond HMG-CoA reductase
    • Gill, S., Stevenson, J., Kristiana, I., Brown, A.J., Cholesterol-dependent degradation of squalene monooxygenase, a control point in cholesterol synthesis beyond HMG-CoA reductase. Cell Metab. 13 (2011), 260–273, 10.1016/j.cmet.2011.01.015.
    • (2011) Cell Metab. , vol.13 , pp. 260-273
    • Gill, S.1    Stevenson, J.2    Kristiana, I.3    Brown, A.J.4
  • 20
    • 30344452931 scopus 로고    scopus 로고
    • Sterol-regulated ubiquitination and degradation of Insig-1 creates a convergent mechanism for feedback control of cholesterol synthesis and uptake
    • Gong, Y., Lee, J.N., Lee, P.C., Goldstein, J.L., Brown, M.S., Ye, J., Sterol-regulated ubiquitination and degradation of Insig-1 creates a convergent mechanism for feedback control of cholesterol synthesis and uptake. Cell Metab. 3 (2006), 15–24, 10.1016/j.cmet.2005.11.014.
    • (2006) Cell Metab. , vol.3 , pp. 15-24
    • Gong, Y.1    Lee, J.N.2    Lee, P.C.3    Goldstein, J.L.4    Brown, M.S.5    Ye, J.6
  • 21
    • 84926522124 scopus 로고    scopus 로고
    • Structure of the WD40 domain of SCAP from fission yeast reveals the molecular basis for SREBP recognition
    • Gong, X., Li, J., Shao, W., Wu, J., Qian, H., Ren, R., Espenshade, P., Yan, N., Structure of the WD40 domain of SCAP from fission yeast reveals the molecular basis for SREBP recognition. Cell Res. 25 (2015), 401–411, 10.1038/cr.2015.32.
    • (2015) Cell Res. , vol.25 , pp. 401-411
    • Gong, X.1    Li, J.2    Shao, W.3    Wu, J.4    Qian, H.5    Ren, R.6    Espenshade, P.7    Yan, N.8
  • 23
    • 84948469149 scopus 로고    scopus 로고
    • Dysregulation of plasmalogen homeostasis impairs cholesterol biosynthesis
    • (jbc. M115. 656983)
    • Honsho, M., Abe, Y., Fujiki, Y., Dysregulation of plasmalogen homeostasis impairs cholesterol biosynthesis. J. Biol. Chem. 48 (2015), 28822–28833 (jbc. M115. 656983).
    • (2015) J. Biol. Chem. , vol.48 , pp. 28822-28833
    • Honsho, M.1    Abe, Y.2    Fujiki, Y.3
  • 24
    • 0142027805 scopus 로고    scopus 로고
    • Combined analysis of oligonucleotide microarray data from transgenic and knockout mice identifies direct SREBP target genes
    • Horton, J.D., Shah, N.A., Warrington, J.A., Anderson, N.N., Park, S.W., Brown, M.S., Goldstein, J.L., Combined analysis of oligonucleotide microarray data from transgenic and knockout mice identifies direct SREBP target genes. Proc. Natl. Acad. Sci. U. S. A. 100 (2003), 12027–12032, 10.1073/pnas.1534923100.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 12027-12032
    • Horton, J.D.1    Shah, N.A.2    Warrington, J.A.3    Anderson, N.N.4    Park, S.W.5    Brown, M.S.6    Goldstein, J.L.7
  • 25
    • 84946925425 scopus 로고    scopus 로고
    • The regulatory domain of squalene monooxygenase contains a re-entrant loop and senses cholesterol via a conformational change
    • Howe, V., Chua, N.K., Stevenson, J., Brown, A.J., The regulatory domain of squalene monooxygenase contains a re-entrant loop and senses cholesterol via a conformational change. J. Biol. Chem., 2015, 675181, 10.1074/jbc.M115.
    • (2015) J. Biol. Chem. , pp. 675181
    • Howe, V.1    Chua, N.K.2    Stevenson, J.3    Brown, A.J.4
  • 26
    • 0028960739 scopus 로고
    • Structure of the human gene encoding sterol regulatory element binding protein-1 (SREBF1) and localization of SREBF1 and SREBF2 to chromosomes 17p11.2 and 22q13
    • Hua, X., Wu, J., Goldstein, J.L., Brown, M.S., Hobbs, H.H., Structure of the human gene encoding sterol regulatory element binding protein-1 (SREBF1) and localization of SREBF1 and SREBF2 to chromosomes 17p11.2 and 22q13. Genomics 25 (1995), 667–673.
    • (1995) Genomics , vol.25 , pp. 667-673
    • Hua, X.1    Wu, J.2    Goldstein, J.L.3    Brown, M.S.4    Hobbs, H.H.5
  • 27
    • 84890227773 scopus 로고    scopus 로고
    • Erlins restrict SREBP activation in the ER and regulate cellular cholesterol homeostasis
    • Huber, M.D., Vesely, P.W., Datta, K., Gerace, L., Erlins restrict SREBP activation in the ER and regulate cellular cholesterol homeostasis. J. Cell Biol. 203 (2013), 427–436, 10.1083/jcb.201305076.
    • (2013) J. Cell Biol. , vol.203 , pp. 427-436
    • Huber, M.D.1    Vesely, P.W.2    Datta, K.3    Gerace, L.4
  • 28
    • 84874644958 scopus 로고    scopus 로고
    • Proteome-wide mapping of cholesterol-interacting proteins in mammalian cells
    • Hulce, J.J., Cognetta, A.B., Niphakis, M.J., Tully, S.E., Cravatt, B.F., Proteome-wide mapping of cholesterol-interacting proteins in mammalian cells. Nat. Methods 10 (2013), 259–264, 10.1038/nmeth.2368.
    • (2013) Nat. Methods , vol.10 , pp. 259-264
    • Hulce, J.J.1    Cognetta, A.B.2    Niphakis, M.J.3    Tully, S.E.4    Cravatt, B.F.5
  • 29
    • 0029805887 scopus 로고    scopus 로고
    • An oxysterol signalling pathway mediated by the nuclear receptor LXR alpha
    • Janowski, B.A., Willy, P.J., Devi, T.R., Falck, J.R., Mangelsdorf, D.J., An oxysterol signalling pathway mediated by the nuclear receptor LXR alpha. Nature 383 (1996), 728–731, 10.1038/383728a0.
    • (1996) Nature , vol.383 , pp. 728-731
    • Janowski, B.A.1    Willy, P.J.2    Devi, T.R.3    Falck, J.R.4    Mangelsdorf, D.J.5
  • 31
    • 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., DeBose-Boyd, R.A., Membrane-associated ubiquitin ligase complex containing gp78 mediates sterol-accelerated degradation of 3-Hydroxy-3-methylglutaryl-coenzyme a reductase. J. Biol. Chem. 286 (2011), 15022–15031, 10.1074/jbc.M110.211326.
    • (2011) J. Biol. Chem. , vol.286 , pp. 15022-15031
    • Jo, Y.1    Sguigna, P.V.2    DeBose-Boyd, R.A.3
  • 32
    • 56049125015 scopus 로고    scopus 로고
    • Different kinetics of cholesterol delivery to components of the cholesterol homeostatic machinery: implications for cholesterol trafficking to the endoplasmic reticulum
    • Kristiana, I., Yang, H., Brown, A.J., Different kinetics of cholesterol delivery to components of the cholesterol homeostatic machinery: implications for cholesterol trafficking to the endoplasmic reticulum. Biochim. Biophys. Acta, 2008, 724–730, 10.1016/j.bbalip.2008.08.006.
    • (2008) Biochim. Biophys. Acta , pp. 724-730
    • Kristiana, I.1    Yang, H.2    Brown, A.J.3
  • 33
    • 84866925293 scopus 로고    scopus 로고
    • Cholesterol through the looking glass: ability of its enantiomer also to elicit homeostatic responses
    • Kristiana, I., Luu, W., Stevenson, J., Cartland, S., Jessup, W., Belani, J.D., Rychnovsky, S.D., Brown, A.J., Cholesterol through the looking glass: ability of its enantiomer also to elicit homeostatic responses. J. Biol. Chem. 287 (2012), 33897–33904, 10.1074/jbc.M112.360537.
    • (2012) J. Biol. Chem. , vol.287 , pp. 33897-33904
    • Kristiana, I.1    Luu, W.2    Stevenson, J.3    Cartland, S.4    Jessup, W.5    Belani, J.D.6    Rychnovsky, S.D.7    Brown, A.J.8
  • 34
    • 0036534286 scopus 로고    scopus 로고
    • The sterol-sensing domain: multiple families, a unique role?
    • Kuwabara, P.E., Labouesse, M., The sterol-sensing domain: multiple families, a unique role?. Trends Genet.: TIG 18 (2002), 193–201.
    • (2002) Trends Genet.: TIG , vol.18 , pp. 193-201
    • Kuwabara, P.E.1    Labouesse, M.2
  • 35
    • 0027322412 scopus 로고
    • Role of the plasma membrane in cholesterol esterification in rat hepatoma cells
    • Lange, Y., Strebel, F., Steck, T.L., Role of the plasma membrane in cholesterol esterification in rat hepatoma cells. J. Biol. Chem. 268 (1993), 13838–13843.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13838-13843
    • Lange, Y.1    Strebel, F.2    Steck, T.L.3
  • 36
    • 0033384957 scopus 로고    scopus 로고
    • Regulation of endoplasmic reticulum cholesterol by plasma membrane cholesterol
    • Lange, Y., Ye, J., Rigney, M., Steck, T.L., Regulation of endoplasmic reticulum cholesterol by plasma membrane cholesterol. J. Lipid Res. 40 (1999), 2264–2270.
    • (1999) J. Lipid Res. , vol.40 , pp. 2264-2270
    • Lange, Y.1    Ye, J.2    Rigney, M.3    Steck, T.L.4
  • 37
    • 4143069270 scopus 로고    scopus 로고
    • How cholesterol homeostasis is regulated by plasma membrane cholesterol in excess of phospholipids
    • Lange, Y., Ye, J., Steck, T.L., How cholesterol homeostasis is regulated by plasma membrane cholesterol in excess of phospholipids. Proc. Natl. Acad. Sci. U. S. A. 101 (2004), 11664–11667, 10.1073/pnas.0404766101.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 11664-11667
    • Lange, Y.1    Ye, J.2    Steck, T.L.3
  • 38
    • 38349112601 scopus 로고    scopus 로고
    • Effectors of rapid homeostatic responses of endoplasmic reticulum cholesterol and 3-hydroxy-3-methylglutaryl-CoA reductase
    • Lange, Y., Ory, D.S., Ye, J., Lanier, M.H., Hsu, F.F., Steck, T.L., Effectors of rapid homeostatic responses of endoplasmic reticulum cholesterol and 3-hydroxy-3-methylglutaryl-CoA reductase. J. Biol. Chem. 283 (2008), 1445–1455, 10.1074/jbc.M706967200.
    • (2008) J. Biol. Chem. , vol.283 , pp. 1445-1455
    • Lange, Y.1    Ory, D.S.2    Ye, J.3    Lanier, M.H.4    Hsu, F.F.5    Steck, T.L.6
  • 39
    • 84904254376 scopus 로고    scopus 로고
    • Essentially all excess fibroblast cholesterol moves from plasma membranes to intracellular compartments
    • Lange, Y., Ye, J., Steck, T.L., Essentially all excess fibroblast cholesterol moves from plasma membranes to intracellular compartments. PLoS One, 9, 2014, e98482, 10.1371/journal.pone.0098482.
    • (2014) PLoS One , vol.9 , pp. e98482
    • Lange, Y.1    Ye, J.2    Steck, T.L.3
  • 41
    • 36549034768 scopus 로고    scopus 로고
    • Blood cholesterol and vascular mortality by age, sex, and blood pressure: a meta-analysis of individual data from 61 prospective studies with 55,000 vascular deaths
    • Lewington, S., Whitlock, G., Clarke, R., Sherliker, P., Emberson, J., Halsey, J., Qizilbash, N., Peto, R., Collins, R., Blood cholesterol and vascular mortality by age, sex, and blood pressure: a meta-analysis of individual data from 61 prospective studies with 55,000 vascular deaths. Lancet (London, England) 370 (2007), 1829–1839, 10.1016/s0140-6736(07)61778-4.
    • (2007) Lancet (London, England) , vol.370 , pp. 1829-1839
    • Lewington, S.1    Whitlock, G.2    Clarke, R.3    Sherliker, P.4    Emberson, J.5    Halsey, J.6    Qizilbash, N.7    Peto, R.8    Collins, R.9
  • 42
    • 0031755752 scopus 로고    scopus 로고
    • Peripheral-type benzodiazepine receptor function in cholesterol transport. Identification of a putative cholesterol recognition/interaction amino acid sequence and consensus pattern
    • Li, H., Papadopoulos, V., Peripheral-type benzodiazepine receptor function in cholesterol transport. Identification of a putative cholesterol recognition/interaction amino acid sequence and consensus pattern. Endocrinology 139 (1998), 4991–4997, 10.1210/endo.139.12.6390.
    • (1998) Endocrinology , vol.139 , pp. 4991-4997
    • Li, H.1    Papadopoulos, V.2
  • 45
    • 77955053533 scopus 로고    scopus 로고
    • Cholesterol, the central lipid of mammalian cells
    • Maxfield, F.R., van Meer, G., Cholesterol, the central lipid of mammalian cells. Curr. Opin. Cell Biol. 22 (2010), 422–429, 10.1016/j.ceb.2010.05.004.
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 422-429
    • Maxfield, F.R.1    van Meer, G.2
  • 46
    • 79955973156 scopus 로고    scopus 로고
    • Identification of luminal Loop 1 of Scap protein as the sterol sensor that maintains cholesterol homeostasis
    • Motamed, M., Zhang, Y., Wang, M.L., Seemann, J., Kwon, H.J., Goldstein, J.L., Brown, M.S., Identification of luminal Loop 1 of Scap protein as the sterol sensor that maintains cholesterol homeostasis. J. Biol. Chem. 286 (2011), 18002–18012, 10.1074/jbc.M111.238311.
    • (2011) J. Biol. Chem. , vol.286 , pp. 18002-18012
    • Motamed, M.1    Zhang, Y.2    Wang, M.L.3    Seemann, J.4    Kwon, H.J.5    Goldstein, J.L.6    Brown, M.S.7
  • 47
    • 0036310592 scopus 로고    scopus 로고
    • LXR/RXR activation enhances basolateral efflux of cholesterol in CaCo-2 cells
    • Murthy, S., Born, E., Mathur, S.N., Field, F.J., LXR/RXR activation enhances basolateral efflux of cholesterol in CaCo-2 cells. J. Lipid Res. 43 (2002), 1054–1064.
    • (2002) J. Lipid Res. , vol.43 , pp. 1054-1064
    • Murthy, S.1    Born, E.2    Mathur, S.N.3    Field, F.J.4
  • 49
    • 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
    • Pearce, M.M., Wang, Y., Kelley, G.G., Wojcikiewicz, R.J., SPFH2 mediates the endoplasmic reticulum-associated degradation of inositol 1,4,5-trisphosphate receptors and other substrates in mammalian cells. J. Biol. Chem. 282 (2007), 20104–20115, 10.1074/jbc.M701862200.
    • (2007) J. Biol. Chem. , vol.282 , pp. 20104-20115
    • Pearce, M.M.1    Wang, Y.2    Kelley, G.G.3    Wojcikiewicz, R.J.4
  • 50
    • 0034682556 scopus 로고    scopus 로고
    • Chemical activity of cholesterol in membranes
    • Radhakrishnan, A., McConnell, H.M., Chemical activity of cholesterol in membranes. Biochemistry 39 (2000), 8119–8124.
    • (2000) Biochemistry , vol.39 , pp. 8119-8124
    • Radhakrishnan, A.1    McConnell, H.M.2
  • 51
    • 3242668095 scopus 로고    scopus 로고
    • Direct binding of cholesterol to the purified membrane region of SCAP: mechanism for a sterol-sensing domain
    • Radhakrishnan, A., Sun, L.P., Kwon, H.J., Brown, M.S., Goldstein, J.L., Direct binding of cholesterol to the purified membrane region of SCAP: mechanism for a sterol-sensing domain. Mol. Cell 15 (2004), 259–268, 10.1016/j.molcel.2004.06.019.
    • (2004) Mol. Cell , vol.15 , pp. 259-268
    • Radhakrishnan, A.1    Sun, L.P.2    Kwon, H.J.3    Brown, M.S.4    Goldstein, J.L.5
  • 52
    • 34249848111 scopus 로고    scopus 로고
    • Sterol-regulated transport of SREBPs from endoplasmic reticulum to Golgi: oxysterols block transport by binding to Insig
    • Radhakrishnan, A., Ikeda, Y., Kwon, H.J., Brown, M.S., Goldstein, J.L., Sterol-regulated transport of SREBPs from endoplasmic reticulum to Golgi: oxysterols block transport by binding to Insig. Proc. Natl. Acad. Sci. U. S. A. 104 (2007), 6511–6518, 10.1073/pnas.0700899104.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 6511-6518
    • Radhakrishnan, A.1    Ikeda, Y.2    Kwon, H.J.3    Brown, M.S.4    Goldstein, J.L.5
  • 53
    • 56449110891 scopus 로고    scopus 로고
    • Switch-like control of SREBP-2 transport triggered by small changes in ER cholesterol: a delicate balance
    • Radhakrishnan, A., Goldstein, J.L., McDonald, J.G., Brown, M.S., Switch-like control of SREBP-2 transport triggered by small changes in ER cholesterol: a delicate balance. Cell Metab. 8 (2008), 512–521, 10.1016/j.cmet.2008.10.008.
    • (2008) Cell Metab. , vol.8 , pp. 512-521
    • Radhakrishnan, A.1    Goldstein, J.L.2    McDonald, J.G.3    Brown, M.S.4
  • 54
    • 84937558798 scopus 로고    scopus 로고
    • Protein structure. Crystal structure of a mycobacterial Insig homolog provides insight into how these sensors monitor sterol levels
    • Ren, R., Zhou, X., He, Y., Ke, M., Wu, J., Liu, X., Yan, C., Wu, Y., Gong, X., Lei, S.F., Radhakrishnan, A., Yan, N., Protein structure. Crystal structure of a mycobacterial Insig homolog provides insight into how these sensors monitor sterol levels. Science, 2015, 187–191, 10.1126/science.aab1091.
    • (2015) Science , pp. 187-191
    • Ren, R.1    Zhou, X.2    He, Y.3    Ke, M.4    Wu, J.5    Liu, X.6    Yan, C.7    Wu, Y.8    Gong, X.9    Lei, S.F.10    Radhakrishnan, A.11    Yan, N.12
  • 55
    • 0030604717 scopus 로고    scopus 로고
    • Sterol-regulated release of SREBP-2 from cell membranes requires two sequential cleavages: one within a transmembrane segment
    • Sakai, J., Duncan, E.A., Rawson, R.B., Hua, X., Brown, M.S., Goldstein, J.L., Sterol-regulated release of SREBP-2 from cell membranes requires two sequential cleavages: one within a transmembrane segment. Cell 85 (1996), 1037–1046.
    • (1996) Cell , vol.85 , pp. 1037-1046
    • Sakai, J.1    Duncan, E.A.2    Rawson, R.B.3    Hua, X.4    Brown, M.S.5    Goldstein, J.L.6
  • 56
    • 0030854859 scopus 로고    scopus 로고
    • Identification of complexes between the COOH-terminal domains of sterol regulatory element-binding proteins (SREBPs) and SREBP cleavage-activating protein
    • Sakai, J., Nohturfft, A., Cheng, D., Ho, 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. 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
  • 57
    • 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., DeBose-Boyd, R.A., Accelerated degradation of HMG CoA reductase mediated by binding of insig-1 to its sterol-Sensing domain. Mol. Cell 11 (2003), 25–33, 10.1016/S1097-2765(02)00822-5.
    • (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
  • 58
    • 84941114077 scopus 로고    scopus 로고
    • Cholesterol sensing by the ABCG1 lipid transporter: requirement of a CRAC motif in the final transmembrane domain
    • Sharpe, L.J., Rao, G., Jones, P.M., Glancey, E., Aleidi, S.M., George, A.M., Brown, A.J., Gelissen, I.C., Cholesterol sensing by the ABCG1 lipid transporter: requirement of a CRAC motif in the final transmembrane domain. Biochim. Biophys. Acta, 2015, 956–964, 10.1016/j.bbalip.2015.02.016.
    • (2015) Biochim. Biophys. Acta , pp. 956-964
    • Sharpe, L.J.1    Rao, G.2    Jones, P.M.3    Glancey, E.4    Aleidi, S.M.5    George, A.M.6    Brown, A.J.7    Gelissen, I.C.8
  • 59
    • 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., Goldstein, J.L., Overproduction of cholesterol and fatty acids causes massive liver enlargement in transgenic mice expressing truncated SREBP-1a. J. Clin. Invest. 98 (1996), 1575–1584, 10.1172/jci118951.
    • (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
  • 60
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K., Ikonen, E., Functional rafts in cell membranes. Nature 387 (1997), 569–572, 10.1038/42408.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 61
    • 3142654791 scopus 로고    scopus 로고
    • Ubiquitination of 3-hydroxy-3-methylglutaryl-CoA reductase in permeabilized cells mediated by cytosolic E1 and a putative membrane-bound ubiquitin ligase
    • Song, B.L., DeBose-Boyd, R.A., Ubiquitination of 3-hydroxy-3-methylglutaryl-CoA reductase in permeabilized cells mediated by cytosolic E1 and a putative membrane-bound ubiquitin ligase. J. Biol. Chem. 279 (2004), 28798–28806, 10.1074/jbc.M402442200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 28798-28806
    • Song, B.L.1    DeBose-Boyd, R.A.2
  • 62
    • 18544378347 scopus 로고    scopus 로고
    • Insig-mediated degradation of HMG CoA reductase stimulated by lanosterol, an intermediate in the synthesis of cholesterol
    • Song, B.L., Javitt, N.B., DeBose-Boyd, R.A., Insig-mediated degradation of HMG CoA reductase stimulated by lanosterol, an intermediate in the synthesis of cholesterol. Cell Metab. 1 (2005), 179–189, 10.1016/j.cmet.2005.01.001.
    • (2005) Cell Metab. , vol.1 , pp. 179-189
    • Song, B.L.1    Javitt, N.B.2    DeBose-Boyd, R.A.3
  • 63
    • 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., DeBose-Boyd, R.A., Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase. Mol. Cell 19 (2005), 829–840, 10.1016/j.molcel.2005.08.009.
    • (2005) Mol. Cell , vol.19 , pp. 829-840
    • Song, B.L.1    Sever, N.2    DeBose-Boyd, R.A.3
  • 64
    • 84904095534 scopus 로고    scopus 로고
    • Squalene mono-oxygenase, a key enzyme in cholesterol synthesis, is stabilized by unsaturated fatty acids
    • Stevenson, J., Luu, W., Kristiana, I., Brown, A.J., Squalene mono-oxygenase, a key enzyme in cholesterol synthesis, is stabilized by unsaturated fatty acids. Biochem. J. 461 (2014), 435–442, 10.1042/BJ20131404.
    • (2014) Biochem. J. , vol.461 , pp. 435-442
    • Stevenson, J.1    Luu, W.2    Kristiana, I.3    Brown, A.J.4
  • 65
    • 22544466429 scopus 로고    scopus 로고
    • Insig required for sterol-mediated inhibition of Scap/SREBP binding to COPII proteins in vitro
    • Sun, L.P., Li, L., Goldstein, J.L., Brown, M.S., Insig required for sterol-mediated inhibition of Scap/SREBP binding to COPII proteins in vitro. J. Biol. Chem. 280 (2005), 26483–26490, 10.1074/jbc.M504041200.
    • (2005) J. Biol. Chem. , vol.280 , pp. 26483-26490
    • Sun, L.P.1    Li, L.2    Goldstein, J.L.3    Brown, M.S.4
  • 66
    • 34249861927 scopus 로고    scopus 로고
    • Sterol-regulated transport of SREBPs from endoplasmic reticulum to Golgi: insig renders sorting signal in Scap inaccessible to COPII proteins
    • Sun, L.P., Seemann, J., Goldstein, J.L., Brown, M.S., Sterol-regulated transport of SREBPs from endoplasmic reticulum to Golgi: insig renders sorting signal in Scap inaccessible to COPII proteins. Proc. Natl. Acad. Sci. U. S. A. 104 (2007), 6519–6526, 10.1073/pnas.0700907104.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 6519-6526
    • Sun, L.P.1    Seemann, J.2    Goldstein, J.L.3    Brown, M.S.4
  • 67
    • 0000727177 scopus 로고
    • Defective cholesterol biosynthesis associated with the Smith-Lemli-Opitz syndrome
    • Tint, G.S., Irons, M., Elias, E.R., Batta, A.K., Frieden, R., Chen, T.S., Salen, G., Defective cholesterol biosynthesis associated with the Smith-Lemli-Opitz syndrome. N. Engl. J. Med. 330 (1994), 107–113, 10.1056/nejm199401133300205.
    • (1994) N. Engl. J. Med. , vol.330 , pp. 107-113
    • Tint, G.S.1    Irons, M.2    Elias, E.R.3    Batta, A.K.4    Frieden, R.5    Chen, T.S.6    Salen, G.7
  • 68
    • 14644395532 scopus 로고    scopus 로고
    • The enantiomer of cholesterol
    • Westover, E.J., Covey, D.F., The enantiomer of cholesterol. J. Membr. Biol. 202 (2004), 61–72, 10.1007/s00232-004-0714-7.
    • (2004) J. Membr. Biol. , vol.202 , pp. 61-72
    • Westover, E.J.1    Covey, D.F.2
  • 70
    • 33845748205 scopus 로고    scopus 로고
    • SREBP-2 positively regulates transcription of the cholesterol efflux gene, ABCA1 by generating oxysterol ligands for LXR
    • Wong, J., Quinn, C.M., Brown, A.J., SREBP-2 positively regulates transcription of the cholesterol efflux gene, ABCA1 by generating oxysterol ligands for LXR. Biochem. J. 400 (2006), 485–491.
    • (2006) Biochem. J. , vol.400 , pp. 485-491
    • Wong, J.1    Quinn, C.M.2    Brown, A.J.3
  • 71
    • 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. U. S. A. 99 (2002), 12753–12758, 10.1073/pnas.162488899.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 12753-12758
    • Yabe, D.1    Brown, M.S.2    Goldstein, J.L.3
  • 72
    • 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
  • 73
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
    • Ye, Y., Meyer, H.H., Rapoport, T.A., The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature 414 (2001), 652–656, 10.1038/414652a.
    • (2001) Nature , vol.414 , pp. 652-656
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 74
    • 67650092919 scopus 로고    scopus 로고
    • LXR regulates cholesterol uptake through Idol-dependent ubiquitination of the LDL receptor
    • Zelcer, N., Hong, C., Boyadjian, R., Tontonoz, P., LXR regulates cholesterol uptake through Idol-dependent ubiquitination of the LDL receptor. Science 325 (2009), 100–104, 10.1126/science.1168974.
    • (2009) Science , vol.325 , pp. 100-104
    • Zelcer, N.1    Hong, C.2    Boyadjian, R.3    Tontonoz, P.4
  • 75
    • 84895820661 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase MARCH6 degrades squalene monooxygenase and affects 3-hydroxy-3-methyl-glutaryl coenzyme A reductase and the cholesterol synthesis pathway
    • Zelcer, N., Sharpe, L.J., Loregger, A., Kristiana, I., Cook, E.C., Phan, L., Stevenson, J., Brown, A.J., The E3 ubiquitin ligase MARCH6 degrades squalene monooxygenase and affects 3-hydroxy-3-methyl-glutaryl coenzyme A reductase and the cholesterol synthesis pathway. Mol. Cell. Biol. 34 (2014), 1262–1270, 10.1128/MCB.01140-13.
    • (2014) Mol. Cell. Biol. , vol.34 , pp. 1262-1270
    • Zelcer, N.1    Sharpe, L.J.2    Loregger, A.3    Kristiana, I.4    Cook, E.C.5    Phan, L.6    Stevenson, J.7    Brown, A.J.8
  • 76
    • 84877883035 scopus 로고    scopus 로고
    • Point mutation in luminal loop 7 of Scap protein blocks interaction with loop 1 and abolishes movement to Golgi
    • Zhang, Y., Motamed, M., Seemann, J., Brown, M.S., Goldstein, J.L., Point mutation in luminal loop 7 of Scap protein blocks interaction with loop 1 and abolishes movement to Golgi. J. Biol. Chem. 288 (2013), 14059–14067, 10.1074/jbc.M113.469528.
    • (2013) J. Biol. Chem. , vol.288 , pp. 14059-14067
    • Zhang, Y.1    Motamed, M.2    Seemann, J.3    Brown, M.S.4    Goldstein, J.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.