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Toward the function of mammalian ATG12-ATG5-ATG16L1 complex in autophagy and related processes
Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.ORCID iD: 0000-0001-5123-135X
2019 (English)In: Autophagy, ISSN 1554-8627, E-ISSN 1554-8635Article in journal (Refereed) Epub ahead of print
Abstract [en]

The machinery that decorates autophagic membranes with lipid-conjugated LC3/GABARAP is not yet fully understood. We recently reported the purification of the full-length ATG12-ATG5-ATG16L1 complex, and in reconstitution experiments with purified ATG7, ATG3, and LC3/GABARAP in vitro, together with rescue experiments in knockout cells, important aspects of the complete lipidation reaction were revealed. Hitherto unobserved membrane-binding regions in ATG16L1 were found, contributing to properties that explain the crucial role of this protein in membrane targeting and LC3/GABARAP lipidation in macroautophagy/autophagy and other related processes.

Place, publisher, year, edition, pages
Taylor & Francis Group, 2019.
Keywords [en]
Amphipathic helix, autophagy, endosome, GABARAP, LAP, LC3, lipidation, membrane
National Category
Cell and Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-160610DOI: 10.1080/15548627.2019.1618100ISI: 000470532900001PubMedID: 31122169OAI: oai:DiVA.org:umu-160610DiVA, id: diva2:1329013
Available from: 2019-06-24 Created: 2019-06-24 Last updated: 2019-06-24

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Carlsson, Sven R

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