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Volumn 289, Issue 11, 2014, Pages 7524-7536

Cellular cholesterol regulates ubiquitination and degradation of the cholesterol export proteins ABCA1 and ABCG1

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; CELL CULTURE; CELLS; PROTEINS; PROTEOLYSIS; TRANSCRIPTION;

EID: 84896276954     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.515890     Document Type: Article
Times cited : (62)

References (54)
  • 2
    • 33646867218 scopus 로고    scopus 로고
    • Roles of ATP binding cassette transporters A1 and G1, scavenger receptor BI and membrane lipid domains in cholesterol export from macrophages
    • DOI 10.1097/01.mol.0000226116.35555.eb, PII 0004143320060600000008
    • Jessup, W., Gelissen, I. C., Gaus, K., and Kritharides, L. (2006) Roles of ATP binding cassette transporters A1 and G1, scavenger receptor BI and membrane lipid domains in cholesterol export from macrophages. Curr. Opin. Lipidol. 17, 247-257 (Pubitemid 43786058)
    • (2006) Current Opinion in Lipidology , vol.17 , Issue.3 , pp. 247-257
    • Jessup, W.1    Gelissen, I.C.2    Gaus, K.3    Kritharides, L.4
  • 4
    • 33845748205 scopus 로고    scopus 로고
    • SREBP-2 positively regulates transcription of the cholesterol efflux gene, ABCA1, by generating oxysterol ligands for LXR
    • DOI 10.1042/BJ20060914
    • Wong J, Quinn CM, and Brown, A. J. (2006) SREBP-2 positively regulates transcription of the cholesterol efflux gene, ABCA1, by generating oxysterol ligands for LXR. Biochem. J. 400, 485-491 (Pubitemid 44974460)
    • (2006) Biochemical Journal , vol.400 , Issue.3 , pp. 485-491
    • Wong, J.1    Quinn, C.M.2    Brown, A.J.3
  • 8
    • 0037151002 scopus 로고    scopus 로고
    • Helical apolipoproteins stabilize ATP-binding cassette transporter A1 by protecting it from thiol protease-mediated degradation
    • DOI 10.1074/jbc.M202996200
    • Arakawa, R., and Yokoyama, S. (2002) Helical apolipoproteins stabilize ATP-binding cassette transporter A1 by protecting it from thiol protease-mediated degradation. J. Biol. Chem. 277, 22426-22429 (Pubitemid 34967213)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.25 , pp. 22426-22429
    • Arakawa, R.1    Yokoyama, S.2
  • 9
    • 0037085289 scopus 로고    scopus 로고
    • Unsaturated fatty acids inhibit cholesterol efflux from macrophages by increasing degradation of ATP-binding cassette transporter A1
    • DOI 10.1074/jbc.M109977200
    • Wang, Y., and Oram, J. F. (2002) Unsaturated fatty acids inhibit cholesterol efflux from macrophages by increasing degradation of ATP-binding cassette transporter A1. J. Biol. Chem. 277, 5692-5697 (Pubitemid 34968625)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.7 , pp. 5692-5697
    • Wang, Y.1    Oram, J.F.2
  • 10
    • 49649095715 scopus 로고    scopus 로고
    • OSBP negatively regulates ABCA1 protein stability
    • Bowden, K., and Ridgway, N. D. (2008) OSBP negatively regulates ABCA1 protein stability. J. Biol. Chem. 283, 18210-18217
    • (2008) J. Biol. Chem. , vol.283 , pp. 18210-18217
    • Bowden, K.1    Ridgway, N.D.2
  • 12
    • 53449092580 scopus 로고    scopus 로고
    • 12/15-Lipoxygenase activity increases the degradation of macrophage ATP-binding cassette transporter G1
    • Nagelin, M. H., Srinivasan, S., Lee, J., Nadler, J. L., and Hedrick, C. C. (2008) 12/15-Lipoxygenase activity increases the degradation of macrophage ATP-binding cassette transporter G1. Arterioscler. Thromb. Vasc. Biol. 28, 1811-1819
    • (2008) Arterioscler. Thromb. Vasc. Biol. , vol.28 , pp. 1811-1819
    • Nagelin, M.H.1    Srinivasan, S.2    Lee, J.3    Nadler, J.L.4    Hedrick, C.C.5
  • 13
    • 71449105303 scopus 로고    scopus 로고
    • Murine 12/15-lipoxygenase regulates ATP-binding cassette transporter G1 protein degradation through p38- and JNK2-dependent pathways
    • Nagelin, M. H., Srinivasan, S., Nadler, J. L., and Hedrick, C. C. (2009) Murine 12/15-lipoxygenase regulates ATP-binding cassette transporter G1 protein degradation through p38- and JNK2-dependent pathways. J. Biol. Chem. 284, 31303-31314
    • (2009) J. Biol. Chem. , vol.284 , pp. 31303-31314
    • Nagelin, M.H.1    Srinivasan, S.2    Nadler, J.L.3    Hedrick, C.C.4
  • 14
    • 84872390119 scopus 로고    scopus 로고
    • Species variation in ABCG1 isoform expression. Implications for the use of animal models in elucidating ABCG1 function
    • Burns, V., Sharpe, L. J., Gelissen, I. C., and Brown, A. J. (2013) Species variation in ABCG1 isoform expression. Implications for the use of animal models in elucidating ABCG1 function. Atherosclerosis 226, 408-411
    • (2013) Atherosclerosis , vol.226 , pp. 408-411
    • Burns, V.1    Sharpe, L.J.2    Gelissen, I.C.3    Brown, A.J.4
  • 17
    • 0037044747 scopus 로고    scopus 로고
    • ABCA1-mediated cholesterol efflux is defective in free cholesterol-loaded macrophages: Mechanism involves enhanced ABCA1 degradation in a process requiring full NPC1 activity
    • DOI 10.1074/jbc.M207532200
    • Feng, B., and Tabas, I. (2002) ABCA1-mediated cholesterol efflux is defective in free cholesterol-loaded macrophages. Mechanism involves enhanced ABCA1 degradation in a process requiring full NPC1 activity. J. Biol. Chem. 277, 43271-43280 (Pubitemid 35285714)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.45 , pp. 43271-43280
    • Feng, B.1    Tabas, I.2
  • 18
    • 0030008367 scopus 로고    scopus 로고
    • Sterol efflux is impaired from macrophage foam cells selectively enriched with 7-ketocholesterol
    • Gelissen, I. C., Brown, A. J., Mander, E. L., Kritharides, L., Dean, R. T., and Jessup, W. (1996) Sterol efflux is impaired from macrophage foam cells selectively enriched with 7-ketocholesterol. J. Biol. Chem. 271, 17852- 17860
    • (1996) J. Biol. Chem. , vol.271 , pp. 17852-17860
    • Gelissen, I.C.1    Brown, A.J.2    Mander, E.L.3    Kritharides, L.4    Dean, R.T.5    Jessup, W.6
  • 21
    • 0036671360 scopus 로고    scopus 로고
    • Cholesterol addition to ER membranes alters conformation of SCAP, the SREBP escort protein that regulates cholesterol metabolism
    • DOI 10.1016/S1097-2765(02)00591-9
    • Brown, A. J., Sun, L., Feramisco, J. D., Brown, M. S., and Goldstein, J. L. (2002) Cholesterol addition to ER membranes alters conformation of SCAP, the SREBP escort protein that regulates cholesterol metabolism. Mol. Cell 10, 237-245 (Pubitemid 35007339)
    • (2002) Molecular Cell , vol.10 , Issue.2 , pp. 237-245
    • Brown, A.J.1    Sun, L.2    Feramisco, J.D.3    Brown, M.S.4    Goldstein, J.L.5
  • 22
    • 0031043937 scopus 로고    scopus 로고
    • Regulation of serum-induced lipid accumulation in human monocyte-derived macrophages by interferon-γ. Correlations with apolipoprotein E production, lipoprotein lipase activity and LDL receptor-related protein expression
    • DOI 10.1016/S0021-9150(96)05979-5, PII S0021915096059795
    • Garner, B., Baoutina, A., Dean, R. T., and Jessup, W. (1997) Regulation of serum-induced lipid accumulation in human monocyte-derived macrophages by interferon-γ. Correlations with apolipoprotein E production, lipoprotein lipase activity and LDL receptor-related protein expression. Atherosclerosis 128, 47-58 (Pubitemid 27065260)
    • (1997) Atherosclerosis , vol.128 , Issue.1 , pp. 47-58
    • Garner, B.1    Baoutina, A.2    Dean, R.T.3    Jessup, W.4
  • 25
    • 79953058037 scopus 로고    scopus 로고
    • Calpain-mediated cleavage negatively regulates the expression level of ABCG1
    • Hori, N., Hayashi, H., and Sugiyama, Y. (2011) Calpain-mediated cleavage negatively regulates the expression level of ABCG1. Atherosclerosis 215, 383-391
    • (2011) Atherosclerosis , vol.215 , pp. 383-391
    • Hori, N.1    Hayashi, H.2    Sugiyama, Y.3
  • 26
    • 0035805621 scopus 로고    scopus 로고
    • ATP-binding cassette transporter A1 contains an NH2-terminal signal anchor sequence that translocates the protein's first hydrophilic domain to the exoplasmic space
    • Fitzgerald, M. L., Mendez, A. J., Moore, K. J., Andersson, L. P., Panjeton, H. A., and Freeman, M. W. (2001) ATP-binding cassette transporter A1 contains an NH2-terminal signal anchor sequence that translocates the protein's first hydrophilic domain to the exoplasmic space. J. Biol. Chem. 276, 15137-15145
    • (2001) J. Biol. Chem. , vol.276 , pp. 15137-15145
    • Fitzgerald, M.L.1    Mendez, A.J.2    Moore, K.J.3    Andersson, L.P.4    Panjeton, H.A.5    Freeman, M.W.6
  • 27
    • 84866382901 scopus 로고    scopus 로고
    • Cholesterol accumulation inhibits ER to Golgi transport and protein secretion. Studies of apolipoprotein E and VSVGt
    • Kockx, M., Dinnes, D. L., Huang, K. Y., Sharpe, L. J., Jessup, W., Brown, A. J., and Kritharides, L. (2012) Cholesterol accumulation inhibits ER to Golgi transport and protein secretion. Studies of apolipoprotein E and VSVGt. Biochem. J. 447, 51-60
    • (2012) Biochem. J. , vol.447 , pp. 51-60
    • Kockx, M.1    Dinnes, D.L.2    Huang, K.Y.3    Sharpe, L.J.4    Jessup, W.5    Brown, A.J.6    Kritharides, L.7
  • 29
    • 0032502719 scopus 로고    scopus 로고
    • Lactacystin, proteasome function, and cell fate
    • DOI 10.1074/jbc.273.15.8545
    • Fenteany, G., and Schreiber, S. L. (1998) Lactacystin, proteasome function, and cell fate. J. Biol. Chem. 273, 8545-8548 (Pubitemid 28176125)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.15 , pp. 8545-8548
    • Fenteany, G.1    Schreiber, S.L.2
  • 30
    • 33749063446 scopus 로고    scopus 로고
    • Macrophage ABCG1 deletion disrupts lipid homeostasis in alveolar macrophages and moderately influences atherosclerotic lesion development in LDL receptor-deficient mice
    • DOI 10.1161/01.ATV.0000237629.29842.4c, PII 0004360520061000000021
    • Out, R., Hoekstra, M., Hildebrand, R. B., Kruit, J. K., Meurs, I., Li, Z., Kuipers, F., Van Berkel, T. J., and Van Eck, M. (2006) Macrophage ABCG1 deletion disrupts lipid homeostasis in alveolar macrophages and moderately influences atherosclerotic lesion development in LDL receptor-deficient mice. Arterioscler. Thromb. Vasc. Biol. 26, 2295-2300 (Pubitemid 44465725)
    • (2006) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.26 , Issue.10 , pp. 2295-2300
    • Out, R.1    Hoekstra, M.2    Hildebrand, R.B.3    Kruit, J.K.4    Meurs, I.5    Li, Z.6    Kuipers, F.7    Van Berkel, T.J.C.8    Van Eck, M.9
  • 32
    • 36849011221 scopus 로고    scopus 로고
    • Combined deficiency of ABCA1 and ABCG1 promotes foam cell accumulation and accelerates atherosclerosis in mice
    • DOI 10.1172/JCI33372
    • Yvan-Charvet, L., Ranalletta, M., Wang, N., Han, S., Terasaka, N., Li, R., Welch, C., and Tall, A. R. (2007) Combined deficiency of ABCA1 and ABCG1 promotes foam cell accumulation and accelerates atherosclerosis in mice. J. Clin. Invest. 117, 3900-3908 (Pubitemid 350224099)
    • (2007) Journal of Clinical Investigation , vol.117 , Issue.12 , pp. 3900-3908
    • Yvan-Charvet, L.1    Ranalletta, M.2    Wang, N.3    Han, S.4    Terasaka, N.5    Li, R.6    Welch, C.7    Tall, A.R.8
  • 33
    • 57649233033 scopus 로고    scopus 로고
    • Direct interaction of nuclear liver X receptor-beta with ABCA1 modulates cholesterol efflux
    • Hozoji, M., Munehira, Y., Ikeda, Y., Makishima, M., Matsuo, M., Kioka, N., and Ueda, K. (2008) Direct interaction of nuclear liver X receptor-beta with ABCA1 modulates cholesterol efflux. J. Biol. Chem. 283, 30057-30063
    • (2008) J. Biol. Chem. , vol.283 , pp. 30057-30063
    • Hozoji, M.1    Munehira, Y.2    Ikeda, Y.3    Makishima, M.4    Matsuo, M.5    Kioka, N.6    Ueda, K.7
  • 34
    • 56749176947 scopus 로고    scopus 로고
    • One step at a time. Endoplasmic reticulum-associated degradation
    • Vembar, S. S., and Brodsky, J. L. (2008) One step at a time. Endoplasmic reticulum-associated degradation. Nat. Rev. Mol. Cell Biol. 9, 944-957
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 944-957
    • Vembar, S.S.1    Brodsky, J.L.2
  • 35
    • 63649086486 scopus 로고    scopus 로고
    • The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins
    • Raiborg, C., and Stenmark, H. (2009) The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins. Nature 458, 445-452
    • (2009) Nature , vol.458 , pp. 445-452
    • Raiborg, C.1    Stenmark, H.2
  • 36
    • 84858121800 scopus 로고    scopus 로고
    • The role of ubiquitylation in receptor endocytosis and endosomal sorting
    • Haglund, K., and Dikic, I. (2012) The role of ubiquitylation in receptor endocytosis and endosomal sorting. J. Cell Sci. 125, 265-275
    • (2012) J. Cell Sci. , vol.125 , pp. 265-275
    • Haglund, K.1    Dikic, I.2
  • 37
    • 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., and Brown, A. J. (2011) Cholesterol-dependent degradation of squalene monooxygenase, a control point in cholesterol synthesis beyond HMG-CoA reductase. Cell Metab. 13, 260-273
    • (2011) Cell Metab. , vol.13 , pp. 260-273
    • Gill, S.1    Stevenson, J.2    Kristiana, I.3    Brown, A.J.4
  • 38
    • 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., and Roitelman, J. (2000) The ubiquitin-proteasome pathway mediates the regulated degradation of mammalian 3-hydroxy-3-methylglutaryl-coenzyme A reductase. J. Biol. Chem. 275, 35840-35847
    • (2000) J. Biol. Chem. , vol.275 , pp. 35840-35847
    • Ravid, T.1    Doolman, R.2    Avner, R.3    Harats, D.4    Roitelman, J.5
  • 39
    • 75149146624 scopus 로고    scopus 로고
    • The TRC8 ubiquitin ligase is sterol regulated and interacts with lipid and protein biosynthetic pathways
    • Lee, J. P., Brauweiler, A., Rudolph, M., Hooper, J. E., Drabkin, H. A., and Gemmill, R. M. (2010) The TRC8 ubiquitin ligase is sterol regulated and interacts with lipid and protein biosynthetic pathways. Mol. Cancer Res. 8, 93-106
    • (2010) Mol. Cancer Res. , vol.8 , pp. 93-106
    • Lee, J.P.1    Brauweiler, A.2    Rudolph, M.3    Hooper, J.E.4    Drabkin, H.A.5    Gemmill, R.M.6
  • 41
    • 0038448097 scopus 로고    scopus 로고
    • Regulation and mechanisms of ATP-binding cassette transporter A1-mediated cellular cholesterol efflux
    • DOI 10.1161/01.ATV.0000075912.83860.26
    • Wang, N., and Tall, A. R. (2003) Regulation and mechanisms of ATP-binding cassette transporter A1-mediated cellular cholesterol efflux. Arterioscler. Thromb. Vasc. Biol. 23, 1178-1184 (Pubitemid 36871270)
    • (2003) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.23 , Issue.7 , pp. 1178-1184
    • Wang, N.1    Tall, A.R.2
  • 44
    • 67650092919 scopus 로고    scopus 로고
    • LXR regulates cholesterol uptake through Idol-dependent ubiquitination of the LDL receptor
    • Zelcer, N., Hong, C., Boyadjian, R., and Tontonoz, P. (2009) LXR regulates cholesterol uptake through Idol-dependent ubiquitination of the LDL receptor. Science 325, 100-104
    • (2009) Science , vol.325 , pp. 100-104
    • Zelcer, N.1    Hong, C.2    Boyadjian, R.3    Tontonoz, P.4
  • 46
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward, C. L., Omura, S., and Kopito, R. R. (1995) Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 83, 121-127
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 50
    • 0028901372 scopus 로고
    • Apolipo-protein A-I-mediated efflux of sterols from oxidized LDL-loaded macrophages
    • Kritharides, L., Jessup, W., Mander, E. L., and Dean, R. T. (1995) Apolipo-protein A-I-mediated efflux of sterols from oxidized LDL-loaded macrophages. Arterioscler. Thromb. Vasc. Biol. 15, 276-289
    • (1995) Arterioscler. Thromb. Vasc. Biol. , vol.15 , pp. 276-289
    • Kritharides, L.1    Jessup, W.2    Mander, E.L.3    Dean, R.T.4
  • 51
    • 79960727241 scopus 로고    scopus 로고
    • Ubiquitination is associated with lysosomal degradation of cell surface-resident ATP-binding cassette transporter A1 (ABCA1) through the endosomal sorting complex required for transport (ESCRT) pathway
    • Mizuno, T., Hayashi, H., Naoi, S., and Sugiyama, Y. (2011) Ubiquitination is associated with lysosomal degradation of cell surface-resident ATP-binding cassette transporter A1 (ABCA1) through the endosomal sorting complex required for transport (ESCRT) pathway. Hepatology 54, 631-643
    • (2011) Hepatology , vol.54 , pp. 631-643
    • Mizuno, T.1    Hayashi, H.2    Naoi, S.3    Sugiyama, Y.4
  • 53
    • 1342282993 scopus 로고    scopus 로고
    • Phosphorylation and Stabilization of ATP Binding Cassette Transporter A1 by Synthetic Amphiphilic Helical Peptides
    • DOI 10.1074/jbc.C300553200
    • Arakawa, R., Hayashi, M., Remaley, A. T., Brewer, B. H., Yamauchi, Y., and Yokoyama, S. (2004) Phosphorylation and stabilization of ATP binding cassette transporter A1 by synthetic amphiphilic helical peptides. J. Biol. Chem. 279, 6217-6220 (Pubitemid 38248753)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.8 , pp. 6217-6220
    • Arakawa, R.1    Hayashi, M.2    Remaley, A.T.3    Brewer, B.H.4    Yamauchi, Y.5    Yokoyama, S.6
  • 54
    • 77956826011 scopus 로고    scopus 로고
    • Helical apolipoproteins of high-density lipoprotein enhance phagocytosis by stabilizing ATP-binding cassette transporter A7
    • Tanaka, N., Abe-Dohmae, S., Iwamoto, N., Fitzgerald, M. L., and Yokoyama, S. (2010) Helical apolipoproteins of high-density lipoprotein enhance phagocytosis by stabilizing ATP-binding cassette transporter A7. J. Lipid Res. 51, 2591-2599
    • (2010) J. Lipid Res. , vol.51 , pp. 2591-2599
    • Tanaka, N.1    Abe-Dohmae, S.2    Iwamoto, N.3    Fitzgerald, M.L.4    Yokoyama, S.5


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