Lipidation status of single membrane-associated ATG8 proteins
- PMID: 34154877
- DOI: 10.1016/j.tibs.2021.06.004
Lipidation status of single membrane-associated ATG8 proteins
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.
Keywords: ATG4 proteases; ATG8 proteins; aminoglycerophospholipids; lipidation; noncanonical autophagy; oxidation.
Copyright © 2021 Elsevier Ltd. All rights reserved.
Comment on
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Oxidation inhibits autophagy protein deconjugation from phagosomes to sustain MHC class II restricted antigen presentation.Nat Commun. 2021 Mar 8;12(1):1508. doi: 10.1038/s41467-021-21829-6. Nat Commun. 2021. PMID: 33686057 Free PMC article.
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Non-canonical autophagy drives alternative ATG8 conjugation to phosphatidylserine.Mol Cell. 2021 May 6;81(9):2031-2040.e8. doi: 10.1016/j.molcel.2021.03.020. Epub 2021 Apr 27. Mol Cell. 2021. PMID: 33909989 Free PMC article.
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