Toward the function of mammalian ATG12-ATG5-ATG16L1 complex in autophagy and related processes
Alf Håkon Lystad1, Sven R Carlsson2, Anne Simonsen1
1a Department of Molecular Medicine, Institute of Basic Medical Sciences and Centre for Cancer Cell Reprogramming , University of Oslo , Oslo , Norway .
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.
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