Lipidation status of single membrane-associated ATG8 proteins. Issue 10 (October 2021)

• Record Type: Journal Article
• Authors: Viret, Christophe; Faure, Mathias
• Is Part Of: Trends in biochemical sciences. Volume 46:Issue 10(2021)
• Page Start: 787
• Page End: 789
• Publication Date: 2021-10
• Subjects: noncanonical autophagy -- ATG8 proteins -- lipidation -- aminoglycerophospholipids -- oxidation -- ATG4 proteases; Biochemistry -- Periodicals; 572
• DOI: 10.1016/j.tibs.2021.06.004
• Languages: English
• ISSNs: 0968-0004

Abstract

Abstract : ATG8 are core autophagy proteins, the lipidated forms of which decorate double-membraned autophagosomes, as well as single-membraned organelles such as endolysosomes. Recent studies from the Florey and Münz laboratories delineate the status of single membrane-associated ATG8 proteins by indicating that their membrane anchoring can involve phosphatidylserine conjugation and their stabilization depends on ATG4 protease inhibition.