CoChat
Sign Up
Cited by 74

The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.

The UPS and downs of cholesterol homeostasis

Sharpe, Laura J., Cook, Emma C.L., Zelcer, Noam, Brown, Andrew J.·2014·Trends in Biochemical Sciences
DOI 10.1016/j.tibs.2014.08.008
Open this paper in CoChat — free account

Abstract

An emerging theme in the regulation of cholesterol homeostasis is the role of the ubiquitin proteasome system (UPS), through which proteins are ubiquitylated and then degraded in response to specific signals. The UPS controls all aspects of cholesterol metabolism including its synthesis, uptake, and efflux. We review here recent work uncovering the ubiquitylation and degradation of key players in cholesterol homeostasis. This includes the low-density lipoprotein (LDL) receptor, transcription factors (sterol regulatory element binding proteins and liver X receptors), flux-controlling enzymes in cholesterol synthesis (3-hydroxy-3-methylglutaryl-CoA reductase and squalene monooxygenase), and cholesterol exporters (ATP-binding cassette transporters ABCA1 and ABCG1). We explore which E3 ligases are involved, and identify areas deserving of further research.

Overview

Integrity signals

Registry

Crossref · 10.1016/j.tibs.2014.08.008

Cites

10 of 10 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Verification

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Citations

Cites

Flagged first, then by citations

Research works printed but not linked: 72

  1. Hornbeck, 2012, PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse, Nucleic Acids Res., 40, D261, 10.1093/nar/gkr1122 · DOI
  2. Metzger, 2012, HECT and RING finger families of E3 ubiquitin ligases at a glance, J. Cell Sci., 125, 531, 10.1242/jcs.091777 · DOI
  3. Goldstein, 2006, Protein sensors for membrane sterols, Cell, 124, 35, 10.1016/j.cell.2005.12.022 · DOI · Paper page
  4. Sharpe, 2013, Controlling cholesterol synthesis beyond 3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR), J. Biol. Chem., 288, 18707, 10.1074/jbc.R113.479808 · DOI · Paper page
  5. Horton, 2003, Combined analysis of oligonucleotide microarray data from transgenic and knockout mice identifies direct SREBP target genes, Proc. Natl. Acad. Sci. U.S.A., 100, 12027, 10.1073/pnas.1534923100 · DOI · Paper page
  6. Radhakrishnan, 2008, Switch-like control of SREBP-2 transport triggered by small changes in ER cholesterol: a delicate balance, Cell Metab., 8, 512, 10.1016/j.cmet.2008.10.008 · DOI · Paper page
  7. Hirano, 2001, Direct demonstration of rapid degradation of nuclear sterol regulatory element-binding proteins by the ubiquitin-proteasome pathway, J. Biol. Chem., 276, 36431, 10.1074/jbc.M105200200 · DOI · Paper page
  8. Sundqvist, 2005, Control of lipid metabolism by phosphorylation-dependent degradation of the SREBP family of transcription factors by SCF(Fbw7), Cell Metab., 1, 379, 10.1016/j.cmet.2005.04.010 · DOI
  9. Bengoechea-Alonso, 2009, A phosphorylation cascade controls the degradation of active SREBP1, J. Biol. Chem., 284, 5885, 10.1074/jbc.M807906200 · DOI
  10. Punga, 2006, Phosphorylation and ubiquitination of the transcription factor sterol regulatory element-binding protein-1 in response to DNA binding, J. Biol. Chem., 281, 25278, 10.1074/jbc.M604983200 · DOI
  11. Sundqvist, 2003, Transcription-dependent degradation controls the stability of the SREBP family of transcription factors, Proc. Natl. Acad. Sci. U.S.A., 100, 13833, 10.1073/pnas.2335135100 · DOI
  12. Zhao, 2012, Regulation of lipogenesis by cyclin-dependent kinase 8-mediated control of SREBP-1, J. Clin. Invest., 122, 2417, 10.1172/JCI61462 · DOI
  13. Lee, 2014, RNF20 regulates hepatic lipid metabolism through PKA-dependent SREBP1c degradation, Hepatology, 60, 844, 10.1002/hep.27011 · DOI
  14. Giandomenico, 2003, Coactivator-dependent acetylation stabilizes members of the SREBP family of transcription factors, Mol. Cell. Biol., 23, 2587, 10.1128/MCB.23.7.2587-2599.2003 · DOI · Paper page
  15. Ponugoti, 2010, SIRT1 deacetylates and inhibits SREBP-1C activity in regulation of hepatic lipid metabolism, J. Biol. Chem., 285, 33959, 10.1074/jbc.M110.122978 · DOI
  16. Hirano, 2003, Sterol regulatory element-binding proteins are negatively regulated through SUMO-1 modification independent of the ubiquitin/26S proteasome pathway, J. Biol. Chem., 278, 16809, 10.1074/jbc.M212448200 · DOI · Paper page
  17. Lee, 2014, PIASy-mediated sumoylation of SREBP1c regulates hepatic lipid metabolism upon fasting signaling, Mol. Cell. Biol., 34, 926, 10.1128/MCB.01166-13 · DOI
  18. Drabkin, 2012, Cholesterol and the development of clear-cell renal carcinoma, Curr. Opin. Pharmacol., 12, 742, 10.1016/j.coph.2012.08.002 · DOI
  19. Gemmill, 1998, The hereditary renal cell carcinoma 3;8 translocation fuses FHIT to a patched-related gene, TRC8, Proc. Natl. Acad. Sci. U.S.A., 95, 9572, 10.1073/pnas.95.16.9572 · DOI
  20. Brauweiler, 2007, RING-dependent tumor suppression and G2/M arrest induced by the TRC8 hereditary kidney cancer gene, Oncogene, 26, 2263, 10.1038/sj.onc.1210017 · DOI
  21. Irisawa, 2009, The sterol-sensing endoplasmic reticulum (ER) membrane protein TRC8 hampers ER to Golgi transport of sterol regulatory element-binding protein-2 (SREBP-2)/SREBP cleavage-activated protein and reduces SREBP-2 cleavage, J. Biol. Chem., 284, 28995, 10.1074/jbc.M109.041376 · DOI · Paper page
  22. Lee, 2010, The TRC8 ubiquitin ligase is sterol regulated and interacts with lipid and protein biosynthetic pathways, Mol. Cancer Res., 8, 93, 10.1158/1541-7786.MCR-08-0491 · DOI · Paper page
  23. Gill, 2008, Sterol regulators of cholesterol homeostasis and beyond: the oxysterol hypothesis revisited and revised, Prog. Lipid Res., 47, 391, 10.1016/j.plipres.2008.04.002 · DOI
  24. Li, 2007, SIRT1 deacetylates and positively regulates the nuclear receptor LXR, Mol. Cell, 28, 91, 10.1016/j.molcel.2007.07.032 · DOI
  25. Lonard, 2000, The 26S proteasome is required for estrogen receptor-α and coactivator turnover and for efficient estrogen receptor-α transactivation, Mol. Cell, 5, 939, 10.1016/S1097-2765(00)80259-2 · DOI
  26. Dace, 2000, Hormone binding induces rapid proteasome-mediated degradation of thyroid hormone receptors, Proc. Natl. Acad. Sci. U.S.A., 97, 8985, 10.1073/pnas.160257997 · DOI
  27. Kim, 2009, Liver X receptor ligands suppress ubiquitination and degradation of LXRalpha by displacing BARD1/BRCA1, Mol. Endocrinol., 23, 466, 10.1210/me.2008-0295 · DOI
  28. Gill, 2011, Cholesterol-dependent degradation of squalene monooxygenase, a control point in cholesterol synthesis beyond HMG-CoA reductase, Cell Metab., 13, 260, 10.1016/j.cmet.2011.01.015 · DOI · Paper page
  29. Kikkert, 2004, Human HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulum, J. Biol. Chem., 279, 3525, 10.1074/jbc.M307453200 · DOI · Paper page
  30. Luu, 2014, Signaling regulates activity of DHCR24, the final enzyme in cholesterol synthesis, J. Lipid Res., 55, 410, 10.1194/jlr.M043257 · DOI
  31. Gardner, 2001, In vivo action of the HRD ubiquitin ligase complex: mechanisms of endoplasmic reticulum quality control and sterol regulation, Mol. Cell. Biol., 21, 4276, 10.1128/MCB.21.13.4276-4291.2001 · DOI
  32. Song, 2005, Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase, Mol. Cell, 19, 829, 10.1016/j.molcel.2005.08.009 · DOI · Paper page
  33. Tsai, 2012, Differential regulation of HMG-CoA reductase and Insig-1 by enzymes of the ubiquitin-proteasome system, Mol. Biol. Cell, 23, 4484, 10.1091/mbc.E12-08-0631 · DOI
  34. Lee, 2006, Sterol-regulated degradation of Insig-1 mediated by the membrane-bound ubiquitin ligase gp78, J. Biol. Chem., 281, 39308, 10.1074/jbc.M608999200 · DOI
  35. Jo, 2011, Sterol-induced degradation of HMG CoA reductase depends on interplay of two Insigs and two ubiquitin ligases, gp78 and Trc8, Proc. Natl. Acad. Sci. U.S.A., 108, 20503, 10.1073/pnas.1112831108 · DOI
  36. Liu, 2012, Ablation of gp78 in liver improves hyperlipidemia and insulin resistance by inhibiting SREBP to decrease lipid biosynthesis, Cell Metab., 16, 213, 10.1016/j.cmet.2012.06.014 · DOI · Paper page
  37. Zelcer, 2014, 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, 1262, 10.1128/MCB.01140-13 · DOI · Paper page
  38. Kostova, 2007, Ubiquitin ligases, critical mediators of endoplasmic reticulum-associated degradation, Semin. Cell Dev. Biol., 18, 770, 10.1016/j.semcdb.2007.09.002 · DOI
  39. Zavacki, 2009, The E3 ubiquitin ligase TEB4 mediates degradation of type 2 iodothyronine deiodinase, Mol. Cell. Biol., 29, 5339, 10.1128/MCB.01498-08 · DOI
  40. Doblas, 2013, The SUD1 gene encodes a putative E3 ubiquitin ligase and is a positive regulator of 3-hydroxy-3-methylglutaryl coenzyme a reductase activity in Arabidopsis, Plant Cell, 25, 728, 10.1105/tpc.112.108696 · DOI
  41. Stevenson, 2014, Squalene monooxygenase, a key enzyme in cholesterol synthesis, is stabilised by unsaturated fatty acids, Biochem. J., 461, 435, 10.1042/BJ20131404 · DOI
  42. Hulce, 2013, Proteome-wide mapping of cholesterol-interacting proteins in mammalian cells, Nat. Methods, 10, 259, 10.1038/nmeth.2368 · DOI
  43. Kristiana, 2012, Cholesterol through the looking glass: ability of its enantiomer also to elicit homeostatic responses, J. Biol. Chem., 287, 33897, 10.1074/jbc.M112.360537 · DOI
  44. Goldstein, 2009, The LDL receptor, Atertioscler. Thromb. Vasc. Biol., 29, 431, 10.1161/ATVBAHA.108.179564 · DOI · Paper page
  45. Jeong, 2008, Sterol-dependent regulation of proprotein convertase subtilisin/kexin type 9 expression by sterol-regulatory element binding protein-2, J. Lipid Res., 49, 399, 10.1194/jlr.M700443-JLR200 · DOI · Paper page
  46. Costet, 2008, PCSK9 and LDL cholesterol: unravelling the target to design the bullet, Trends Biochem. Sci., 33, 426, 10.1016/j.tibs.2008.06.005 · DOI
  47. Wang, 2012, Molecular characterization of proprotein convertase subtilisin/kexin type 9-mediated degradation of the LDLR, J. Lipid Res., 53, 1932, 10.1194/jlr.M028563 · DOI · Paper page
  48. Holla, 2010, A chimeric LDL receptor containing the cytoplasmic domain of the transferrin receptor is degraded by PCSK9, Mol. Genet. Metab., 99, 149, 10.1016/j.ymgme.2009.09.012 · DOI
  49. Strom, 2010, Disrupted recycling of the low density lipoprotein receptor by PCSK9 is not mediated by residues of the cytoplasmic domain, Mol. Genet. Metab., 101, 76, 10.1016/j.ymgme.2010.05.003 · DOI · Paper page
  50. Zelcer, 2009, LXR regulates cholesterol uptake through Idol-dependent ubiquitination of the LDL receptor, Science, 325, 100, 10.1126/science.1168974 · DOI · Paper page
  51. Sorrentino, 2012, Post-transcriptional regulation of lipoprotein receptors by the E3-ubiquitin ligase inducible degrader of the low-density lipoprotein receptor, Curr. Opin. Lipidol., 23, 213, 10.1097/MOL.0b013e3283532947 · DOI · Paper page
  52. Calkin, 2011, FERM-dependent E3 ligase recognition is a conserved mechanism for targeted degradation of lipoprotein receptors, Proc. Natl. Acad. Sci. U.S.A., 108, 20107, 10.1073/pnas.1111589108 · DOI · Paper page
  53. Gelissen, 2011, Drug targets beyond HMG-CoA reductase: why venture beyond the statins?, Front. Biol., 6, 197, 10.1007/s11515-011-1130-x · DOI
  54. Sawamura, 2009, New Idol for cholesterol reduction?, Clin. Chem., 55, 2082, 10.1373/clinchem.2009.134023 · DOI
  55. Sasaki, 2014, Hepatic overexpression of Idol increases circulating protein convertase subtilisin/kexin type 9 in mice and hamsters via dual mechanisms: sterol regulatory element-binding protein 2 and low-density lipoprotein receptor-dependent pathways, Atertioscler. Thromb. Vasc. Biol., 34, 1171, 10.1161/ATVBAHA.113.302670 · DOI · Paper page
  56. Sorrentino, 2013, Identification of a loss-of-function inducible degrader of the low-density lipoprotein receptor variant in individuals with low circulating low-density lipoprotein, Eur. Heart J., 34, 1292, 10.1093/eurheartj/ehs472 · DOI
  57. Westerterp, 2014, ATP-binding cassette transporters, atherosclerosis, and inflammation, Circ. Res., 114, 157, 10.1161/CIRCRESAHA.114.300738 · DOI
  58. Martinez, 2003, Phosphorylation of a pest sequence in ABCA1 promotes calpain degradation and is reversed by ApoA-I, J. Biol. Chem., 278, 37368, 10.1074/jbc.M307161200 · DOI
  59. Wang, 2003, A PEST sequence in ABCA1 regulates degradation by calpain protease and stabilization of ABCA1 by apoA-I, J. Clin. Invest., 111, 99, 10.1172/JCI200316808 · DOI
  60. Lu, 2008, ApoA-I facilitates ABCA1 recycle/accumulation to cell surface by inhibiting its intracellular degradation and increases HDL generation, Atertioscler. Thromb. Vasc. Biol., 28, 1820, 10.1161/ATVBAHA.108.169482 · DOI
  61. Tang, 2004, Effect of apolipoprotein A-I on ATP binding cassette transporter A1 degradation and cholesterol efflux in THP-1 macrophage-derived foam cells, Acta Biochim. Biophys. Sin., 36, 218, 10.1093/abbs/36.3.218 · DOI
  62. Mizuno, 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, 10.1002/hep.24387 · DOI
  63. Ogura, 2011, Proteasomal inhibition promotes ATP-binding cassette transporter A1 (ABCA1) and ABCG1 expression and cholesterol efflux from macrophages in vitro and in vivo, Atertioscler. Thromb. Vasc. Biol., 31, 1980, 10.1161/ATVBAHA.111.228478 · DOI
  64. Suzuki, 2014, Inhibition of post-translational N-glycosylation by HRD1 that controls the fate of ABCG5/8 transporter, Sci. Rep., 4, 4258, 10.1038/srep04258 · DOI
  65. Hsieh, 2014, Cellular cholesterol regulates ubiquitination and degradation of the cholesterol export proteins ABCA1 and ABCG1, J. Biol. Chem., 289, 7524, 10.1074/jbc.M113.515890 · DOI
  66. Komander, 2009, Breaking the chains: structure and function of the deubiquitinases, Nat. Rev. Mol. Cell Biol., 10, 550, 10.1038/nrm2731 · DOI · Paper page
  67. Clague, 2012, Governance of endocytic trafficking and signaling by reversible ubiquitylation, Dev. Cell, 23, 457, 10.1016/j.devcel.2012.08.011 · DOI
  68. de Bie, 2011, Ubiquitination of E3 ligases: self-regulation of the ubiquitin system via proteolytic and non-proteolytic mechanisms, Cell Death Differ., 18, 1393, 10.1038/cdd.2011.16 · DOI · Paper page
  69. Nakasone, 2014, Endoplasmic reticulum-associated degradation of Niemann–Pick C1: evidence for the role of heat shock proteins and identification of lysine residues that accept ubiquitin, J. Biol. Chem., 289, 19714, 10.1074/jbc.M114.549915 · DOI
  70. Fisher, 2011, Ubiquitination regulates the assembly of VLDL in HepG2 cells and is the committing step of the apoB-100 ERAD pathway, J. Lipid Res., 52, 1170, 10.1194/jlr.M011726 · DOI
  71. Jiang, 2014, Ubiquitin ligases in cholesterol metabolism, Diabetes Metab. J., 38, 171, 10.4093/dmj.2014.38.3.171 · DOI
  72. Ruggiano, 2014, Quality control: ER-associated degradation: protein quality control and beyond, J. Cell Biol., 204, 869, 10.1083/jcb.201312042 · DOI

Cited by

Sorted by citations

Metadata

Authors
Sharpe, L. J., Cook, E. C. L., Zelcer, N., & Brown, A. J.
Venue
Trends in Biochemical Sciences
Publisher
Elsevier BV
Published
2014-11
Volume
39
Issue
11
Pages
527-535
ISSN
0968-0004
DOI
10.1016/j.tibs.2014.08.008
Cited by
74
References
10
Language
en
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review