Atg4 proteolytic activity can be inhibited by Atg1 phosphorylation

• DOI: 10.1038/s41467-017-00302-3
• Publication Date: 2017-08-10T17:47:02Z
• Authors: Jana Sánchez-Wand...; Franziska Kriegen...; Sabrina Rohringer; Martina Schuschnig; Rubén Gómez-Sánchez; Bettina Zens; Susana Abreu; Ralph Hardenberg; David Hollenstein; Jieqiong Gao; Christian Ungermann; Sascha Martens; Claudine Kraft; Fulvio Reggiori
• Keywords: ATG8; Autophagosome; Lipid-anchored protein; Phosphatidylethanolamine; Cysteine protease

The biogenesis of autophagosomes depends on the conjugation Atg8-like proteins with phosphatidylethanolamine. Atg8 processing by cysteine protease Atg4 is required for its covalent linkage to phosphatidylethanolamine, but it also necessary deconjugation from this lipid release membranes. How these two cleavage steps are coordinated unknown. Here we show that phosphorylation Atg1 inhibits function, an event appears exclusively occur at site autophagosome biogenesis. These results consistent a model where Atg8-phosphatidylethanolamine pool essential formation protected least in part while newly synthesized cytoplasmic remains susceptible constitutive processing.The mediates lipidation, biogenesis, triggers membranes, however unclear how coordinated. authors sites.