Toward the function of mammalian ATG12-ATG5-ATG16L1 complex in autophagy and related processes

Alf Håkon Lystad; Sven R Carlsson; Anne Simonsen

doi:10.1080/15548627.2019.1618100

Toward the function of mammalian ATG12-ATG5-ATG16L1 complex in autophagy and related processes

Autophagy. 2019 Aug;15(8):1485-1486. doi: 10.1080/15548627.2019.1618100. Epub 2019 May 23.

Authors

Alf Håkon Lystad¹, Sven R Carlsson², Anne Simonsen¹

Affiliations

¹ a Department of Molecular Medicine, Institute of Basic Medical Sciences and Centre for Cancer Cell Reprogramming , University of Oslo , Oslo , Norway .
² b Department of Medical Biochemistry and Biophysics , University of Umeå , Umeå , Sweden .

Abstract

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.

Keywords: ATG16L1; Amphipathic helix; GABARAP; LAP; LC3; autophagy; endosome; lipidation; membrane.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Animals
Autophagy*
Autophagy-Related Proteins
Mammals
Microtubule-Associated Proteins

Substances

Autophagy-Related Proteins
Microtubule-Associated Proteins