As a matter of fat: Emerging roles of lipid-sensitive E3 ubiquitin ligases.

Publisher: Wiley Country of Publication: United States NLM ID: 8510851 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1521-1878 (Electronic) Linking ISSN: 02659247 NLM ISO Abbreviation: Bioessays Subsets: MEDLINE

Publication: <2005->: Hoboken, N.J. : Wiley
Original Publication: Cambridge, UK : Published for the ICSU Press by Cambridge University Press, c1984-

Ubiquitin-Protein Ligases*/metabolism ; Ubiquitin*/metabolism; Ubiquitination ; Proteasome Endopeptidase Complex/metabolism ; Membrane Lipids

The dynamic structure and composition of lipid membranes need to be tightly regulated to control the vast array of cellular processes from cell and organelle morphology to protein-protein interactions and signal transduction pathways. To maintain membrane integrity, sense-and-response systems monitor and adjust membrane lipid composition to the ever-changing cellular environment, but only a relatively small number of control systems have been described. Here, we explore the emerging role of the ubiquitin-proteasome system in monitoring and maintaining membrane lipid composition. We focus on the ER-resident RNF145 E3 ubiquitin ligase, its role in regulating adiponectin receptor 2 (ADIPOR2), its lipid hydrolase substrate, and the broader implications for understanding the homeostatic processes that fine-tune cellular membrane composition.
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210688/Z/18/Z United Kingdom WT_ Wellcome Trust

Keywords: ADIPOR2; E3 ubiquitin ligases; RNF145; homeoviscous adaption; lipids; protein degradation

EC 2.3.2.27 (Ubiquitin-Protein Ligases)
0 (Ubiquitin)
EC 3.4.25.1 (Proteasome Endopeptidase Complex)
0 (Membrane Lipids)

Date Created: 20231027 Date Completed: 20231122 Latest Revision: 20240228

20240228

10.1002/bies.202300139

37890275