CoChat
Sign Up
Cited by 62

The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.

The ubiquitous role of ubiquitination in lipid metabolism

Loix, Melanie, Zelcer, Noam, Bogie, Jeroen F.J., Hendriks, Jerome J.A.·2024·Trends in Cell Biology
DOI 10.1016/j.tcb.2023.09.001
Open this paper in CoChat — free account

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1016/j.tcb.2023.09.001

Cites

6 of 6 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Flagged first, then by citations

Research works printed but not linked: 87

  1. Mani, 2005, The ubiquitin-proteasome pathway and its role in cancer, J. Clin. Oncol., 23, 4776, 10.1200/JCO.2005.05.081 · DOI
  2. Zheng, 2016, Dysregulation of ubiquitin-proteasome system in neurodegenerative diseases, Front. Aging Neurosci., 8, 303, 10.3389/fnagi.2016.00303 · DOI
  3. Zechner, 2012, FAT SIGNALS – lipases and lipolysis in lipid metabolism and signaling, Cell Metab., 15, 279, 10.1016/j.cmet.2011.12.018 · DOI
  4. Yoon, 2021, Lipid metabolism in sickness and in health: emerging regulators of lipotoxicity, Mol. Cell, 81, 3708, 10.1016/j.molcel.2021.08.027 · DOI
  5. Huang, 2020, Cholesterol metabolism in cancer: mechanisms and therapeutic opportunities, Nat. Metab., 2, 132, 10.1038/s42255-020-0174-0 · DOI
  6. Dai, 2021, Cholesterol metabolism in neurodegenerative diseases: molecular mechanisms and therapeutic targets, Mol. Neurobiol., 58, 2183, 10.1007/s12035-020-02232-6 · DOI
  7. Sharpe, 2014, The UPS and downs of cholesterol homeostasis, Trends Biochem. Sci., 39, 527, 10.1016/j.tibs.2014.08.008 · DOI · Paper page
  8. Yan, 2021, Structural basis for sterol sensing by Scap and Insig, Cell Rep., 35, 10.1016/j.celrep.2021.109299 · DOI · Paper page
  9. 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
  10. Kuan, 2020, Ring finger protein 5 activates sterol regulatory element-binding protein 2 (SREBP2) to promote cholesterol biosynthesis via inducing polyubiquitination of SREBP chaperone SCAP, J. Biol. Chem., 295, 3918, 10.1074/jbc.RA119.011849 · DOI
  11. Gong, 2006, Sterol-regulated ubiquitination and degradation of Insig-1 creates a convergent mechanism for feedback control of cholesterol synthesis and uptake, Cell Metab., 3, 15, 10.1016/j.cmet.2005.11.014 · DOI · Paper page
  12. 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
  13. Cook, 2017, Identification of the ER-resident E3 ubiquitin ligase RNF145 as a novel LXR-regulated gene, PLoS One, 12, 10.1371/journal.pone.0172721 · DOI
  14. Zelcer, 2009, LXR regulates cholesterol uptake through Idol-dependent ubiquitination of the LDL receptor, Science, 325, 100, 10.1126/science.1168974 · DOI · Paper page
  15. 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
  16. Dong, 2021, Interferon-γ decreases ATP-binding cassette subfamily G member 1-mediated cholesterol efflux through small ubiquitin-like modifier/ubiquitin-dependent liver X receptor-α degradation in macrophages, Biotechnol. Appl. Biochem., 68, 1412
  17. Hsieh, 2016, TTC39B deficiency stabilizes LXR reducing both atherosclerosis and steatohepatitis, Nature, 535, 303, 10.1038/nature18628 · DOI
  18. Sever, 2003, Accelerated degradation of HMG CoA reductase mediated by binding of insig-1 to its sterol-sensing domain, Mol. Cell, 11, 25, 10.1016/S1097-2765(02)00822-5 · DOI
  19. Sever, 2003, Insig-dependent ubiquitination and degradation of mammalian 3-hydroxy-3-methylglutaryl-CoA reductase stimulated by sterols and geranylgeraniol, J. Biol. Chem., 278, 52479, 10.1074/jbc.M310053200 · DOI
  20. Loregger, 2017, Haploid mammalian genetic screen identifies UBXD8 as a key determinant of HMGCR degradation and cholesterol biosynthesis, Arterioscler. Thromb. Vasc. Biol., 37, 2064, 10.1161/ATVBAHA.117.310002 · DOI
  21. Menzies, 2018, The sterol-responsive RNF145 E3 ubiquitin ligase mediates the degradation of HMG-CoA reductase together with gp78 and Hrd1, ELife, 7, 10.7554/eLife.40009 · DOI
  22. Lu, 2020, Feeding induces cholesterol biosynthesis via the mTORC1-USP20-HMGCR axis, Nature, 588, 479, 10.1038/s41586-020-2928-y · DOI
  23. 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
  24. Sharpe, 2019, Cholesterol increases protein levels of the E3 ligase MARCH6 and thereby stimulates protein degradation, J. Biol. Chem., 294, 2436, 10.1074/jbc.RA118.005069 · DOI
  25. Scott, 2020, The cholesterol synthesis enzyme lanosterol 14α-demethylase is post-translationally regulated by the E3 ubiquitin ligase MARCH6, Biochem. J., 477, 541, 10.1042/BCJ20190647 · DOI · Paper page
  26. Qian, 2023, Cholesterol synthesis enzyme SC4MOL is fine-tuned by sterols and targeted for degradation by the E3 ligase MARCHF6, J. Lipid Res., 64, 10.1016/j.jlr.2023.100362 · DOI · Paper page
  27. Capell-Hattam, 2020, Twin enzymes, divergent control: the cholesterogenic enzymes DHCR14 and LBR are differentially regulated transcriptionally and post-translationally, J. Biol. Chem., 295, 2850, 10.1074/jbc.RA119.011323 · DOI
  28. Prabhu, 2016, Cholesterol-mediated degradation of 7-dehydrocholesterol reductase switches the balance from cholesterol to vitamin D synthesis, J. Biol. Chem., 291, 8363, 10.1074/jbc.M115.699546 · DOI
  29. Mitsche, 2015, Flux analysis of cholesterol biosynthesis in vivo reveals multiple tissue and cell-type specific pathways, Elife, 4, 10.7554/eLife.07999 · DOI
  30. Zhang, 2013, Both K63 and K48 ubiquitin linkages signal lysosomal degradation of the LDL receptor, J. Lipid Res., 54, 1410, 10.1194/jlr.M035774 · DOI · Paper page
  31. van Loon, 2018, Inactivation of the E3 ubiquitin ligase IDOL attenuates diet-induced obesity and metabolic dysfunction in mice, Arterioscler. Thromb. Vasc. Biol., 38, 1785, 10.1161/ATVBAHA.118.311168 · DOI · Paper page
  32. Chen, 2011, Role of ubiquitination in PCSK9-mediated low-density lipoprotein receptor degradation, Biochem. Biophys. Res. Commun., 415, 515, 10.1016/j.bbrc.2011.10.110 · DOI
  33. 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
  34. Wang, 2017, Cholesterol and fatty acids regulate cysteine ubiquitylation of ACAT2 through competitive oxidation, Nat. Cell Biol., 19, 808, 10.1038/ncb3551 · DOI
  35. Zhu, 2023, P53 deficiency affects cholesterol esterification to exacerbate hepatocarcinogenesis, Hepatology, 77, 1499, 10.1002/hep.32518 · DOI
  36. Ogura, 2011, Proteasomal inhibition promotes ATP-binding cassette transporter A1 (ABCA1) and ABCG1 expression and cholesterol efflux from macrophages in vitro and in vivo, Arterioscler. Thromb. Vasc. Biol., 31, 1980, 10.1161/ATVBAHA.111.228478 · DOI
  37. 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
  38. Aleidi, 2015, The E3 ubiquitin ligases, HUWE1 and NEDD4-1, are involved in the post-translational regulation of the ABCG1 and ABCG4 lipid transporters, J. Biol. Chem., 290, 24604, 10.1074/jbc.M115.675579 · DOI
  39. Aleidi, 2018, The E3 ubiquitin ligase, HECTD1, is involved in ABCA1-mediated cholesterol export from macrophages, Biochim. Biophys. Acta Mol. Cell Biol. Lipids, 1863, 359, 10.1016/j.bbalip.2017.12.011 · DOI
  40. Raghavan, 2018, Protease-activated receptor 1 inhibits cholesterol efflux and promotes atherogenesis via cullin 3-mediated degradation of the ABCA1 transporter, J. Biol. Chem., 293, 10574, 10.1074/jbc.RA118.003491 · DOI
  41. Boro, 2021, Thrombin-Par1 signaling axis disrupts COP9 signalosome subunit 3-mediated ABCA1 stabilization in inducing foam cell formation and atherogenesis, Cell Death Differ., 28, 780, 10.1038/s41418-020-00623-9 · DOI
  42. Grajchen, 2018, The physiology of foamy phagocytes in multiple sclerosis, Acta Neuropathol. Commun., 6, 124, 10.1186/s40478-018-0628-8 · DOI
  43. Matsuo, 2022, ABCA1 and ABCG1 as potential therapeutic targets for the prevention of atherosclerosis, J. Pharmacol. Sci., 148, 197, 10.1016/j.jphs.2021.11.005 · DOI
  44. Hauser, 2000, Degradation of the peroxisome proliferator-activated receptor gamma is linked to ligand-dependent activation, J. Biol. Chem., 275, 18527, 10.1074/jbc.M001297200 · DOI
  45. Floyd, 2002, Interferon-gamma-mediated activation and ubiquitin-proteasome-dependent degradation of PPARgamma in adipocytes, J. Biol. Chem., 277, 4062, 10.1074/jbc.M108473200 · DOI
  46. Kilroy, 2012, The ubiquitin ligase Siah2 regulates PPARγ activity in adipocytes, Endocrinology, 153, 1206, 10.1210/en.2011-1725 · DOI
  47. Han, 2013, Upregulation of SIRT1 by 17β-estradiol depends on ubiquitin-proteasome degradation of PPAR-γ mediated by NEDD4-1, Protein Cell, 4, 310, 10.1007/s13238-013-2124-z · DOI
  48. Ning, 2022, USP22 regulates lipidome accumulation by stabilizing PPARγ in hepatocellular carcinoma, Nat. Commun., 13, 2187, 10.1038/s41467-022-29846-9 · DOI
  49. Hou, 2012, PPARγ is an E3 ligase that induces the degradation of NFκB/p65, Nat. Commun., 3, 1300, 10.1038/ncomms2270 · DOI
  50. 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
  51. Lee, 2014, Ring finger protein20 regulates hepatic lipid metabolism through protein kinase A-dependent sterol regulatory element binding protein1c degradation, Hepatology, 60, 844, 10.1002/hep.27011 · DOI
  52. 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
  53. Qi, 2006, TRB3 links the E3 ubiquitin ligase COP1 to lipid metabolism, Science, 312, 1763, 10.1126/science.1123374 · DOI · Paper page
  54. Zheng, 2022, Ubiquitin specific peptidase 38 promotes the progression of gastric cancer through upregulation of fatty acid synthase, Am. J. Cancer Res., 12, 2686
  55. Tian, 2021, ACLY ubiquitination by CUL3-KLHL25 induces the reprogramming of fatty acid metabolism to facilitate iTreg differentiation, Elife, 10, 10.7554/eLife.62394 · DOI
  56. Kato, 2006, Ubiquitin-proteasome-dependent degradation of mammalian ER stearoyl-CoA desaturase, J. Cell Sci., 119, 2342, 10.1242/jcs.02951 · DOI
  57. Ballweg, 2020, Regulation of lipid saturation without sensing membrane fluidity, Nat. Commun., 11, 756, 10.1038/s41467-020-14528-1 · DOI
  58. Volkmar, 2022, Regulation of membrane fluidity by RNF145-triggered degradation of the lipid hydrolase ADIPOR2, EMBO J., 41, 10.15252/embj.2022110777 · DOI
  59. Smith, 2008, Opposite regulation of CD36 ubiquitination by fatty acids and insulin: effects on fatty acid uptake, J. Biol. Chem., 283, 13578, 10.1074/jbc.M800008200 · DOI
  60. Kim, 2011, Parkin is a lipid-responsive regulator of fat uptake in mice and mutant human cells, J. Clin. Invest., 121, 3701, 10.1172/JCI44736 · DOI
  61. Xia, 2020, Deubiquitination of CD36 by UCHL1 promotes foam cell formation, Cell Death Dis., 11, 636, 10.1038/s41419-020-02888-x · DOI
  62. Zhang, 2020, Inhibition of USP14 suppresses the formation of foam cell by promoting CD36 degradation, J. Cell. Mol. Med., 24, 3292, 10.1111/jcmm.15002 · DOI
  63. Wei, 2018, ER-associated ubiquitin ligase HRD1 programs liver metabolism by targeting multiple metabolic enzymes, Nat. Commun., 9, 3659, 10.1038/s41467-018-06091-7 · DOI
  64. Guo, 2021, HRD1 inhibits fatty acid oxidation and tumorigenesis by ubiquitinating CPT2 in triple-negative breast cancer, Mol. Oncol., 15, 642, 10.1002/1878-0261.12856 · DOI
  65. Zechner, 2017, Cytosolic lipolysis and lipophagy: two sides of the same coin, Nat. Rev. Mol. Cell Biol., 18, 671, 10.1038/nrm.2017.76 · DOI · Paper page
  66. Ghosh, 2016, Ubiquitin ligase COP1 controls hepatic fat metabolism by targeting ATGL for degradation, Diabetes, 65, 3561, 10.2337/db16-0506 · DOI
  67. Sugihara, 2019, The AAA+ ATPase/ubiquitin ligase mysterin stabilizes cytoplasmic lipid droplets, J. Cell Biol., 218, 949, 10.1083/jcb.201712120 · DOI
  68. Sakamaki, 2022, Ubiquitination of phosphatidylethanolamine in organellar membranes, Mol. Cell, 82, 3677, 10.1016/j.molcel.2022.08.008 · DOI
  69. Merklinger, 2022, Phospholipids alter activity and stability of mitochondrial membrane-bound ubiquitin ligase MARCH5, Life Sci. Alliance, 5, 10.26508/lsa.202101309 · DOI
  70. Otten, 2021, Ubiquitylation of lipopolysaccharide by RNF213 during bacterial infection, Nature, 594, 111, 10.1038/s41586-021-03566-4 · DOI
  71. Haidar, 2021, Lipophagy: a new player in CNS disorders, Trends Endocrinol. Metab., 32, 941, 10.1016/j.tem.2021.08.010 · DOI
  72. Robichaud, 2021, Identification of novel lipid droplet factors that regulate lipophagy and cholesterol efflux in macrophage foam cells, Autophagy, 17, 3671, 10.1080/15548627.2021.1886839 · DOI
  73. Nguyen, 2019, N-terminal acetylation and the N-end rule pathway control degradation of the lipid droplet protein PLIN2, J. Biol. Chem., 294, 379, 10.1074/jbc.RA118.005556 · DOI · Paper page
  74. Olzmann, 2013, Spatial regulation of UBXD8 and p97/VCP controls ATGL-mediated lipid droplet turnover, Proc. Natl. Acad. Sci. U. S. A., 110, 1345, 10.1073/pnas.1213738110 · DOI
  75. Nian, 2010, Fat-specific protein 27 undergoes ubiquitin-dependent degradation regulated by triacylglycerol synthesis and lipid droplet formation, J. Biol. Chem., 285, 9604, 10.1074/jbc.M109.043786 · DOI
  76. Spandl, 2011, Ancient ubiquitous protein 1 (AUP1) localizes to lipid droplets and binds the E2 ubiquitin conjugase G2 (Ube2g2) via its G2 binding region, J. Biol. Chem., 286, 5599, 10.1074/jbc.M110.190785 · DOI
  77. Eastman, 2009, A role for ubiquitin ligases and Spartin/SPG20 in lipid droplet turnover, J. Cell Biol., 184, 881, 10.1083/jcb.200808041 · DOI
  78. Zhu, 2022, Regulation of glucose, fatty acid and amino acid metabolism by ubiquitination and SUMOylation for cancer progression, Front. Cell Dev. Biol., 10
  79. Zhou, 2021, The role of ubiquitin E3 ligase in atherosclerosis, Curr. Med. Chem., 28, 152, 10.2174/0929867327666200306124418 · DOI
  80. Choi, 2015, Recapitulating amyloid β and tau pathology in human neural cell culture models: clinical implications, US Neurol., 11, 102
  81. Ivatt, 2014, Genome-wide RNAi screen identifies the Parkinson disease GWAS risk locus SREBF1 as a regulator of mitophagy, Proc. Natl. Acad. Sci. U. S. A., 111, 8494, 10.1073/pnas.1321207111 · DOI · Paper page
  82. Cvek, 2011, The ubiquitin-proteasome system (UPS) and the mechanism of action of bortezomib, Curr. Pharm. Des., 17, 1483, 10.2174/138161211796197124 · DOI
  83. Cohen, 2010, Will the ubiquitin system furnish as many drug targets as protein kinases?, Cell, 143, 686, 10.1016/j.cell.2010.11.016 · DOI
  84. Bedford, 2011, Ubiquitin-like protein conjugation and the ubiquitin–proteasome system as drug targets, Nat. Rev. Drug Discov., 10, 29, 10.1038/nrd3321 · DOI · Paper page
  85. Swatek, 2016, Ubiquitin modifications, Cell Res., 26, 399, 10.1038/cr.2016.39 · DOI
  86. Singh, 2009, Autophagy regulates lipid metabolism, Nature, 458, 1131, 10.1038/nature07976 · DOI · Paper page
  87. Stevenson, 2016, Endoplasmic reticulum-associated degradation and lipid homeostasis, Annu. Rev. Nutr., 36, 511, 10.1146/annurev-nutr-071715-051030 · DOI

Cited by

Sorted by citations

Metadata

Authors
Loix, M., Zelcer, N., Bogie, J. F. J., & Hendriks, J. J. A.
ORCID
Hendriks, Jerome J.A.
Venue
Trends in Cell Biology
Publisher
Elsevier BV
Published
2024-05
Volume
34
Issue
5
Pages
416-429
ISSN
0962-8924
DOI
10.1016/j.tcb.2023.09.001
Cited by
62
References
6
Language
en
Licence

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