Atg4 proteolytic activity can be inhibited by Atg1 phosphorylation

Jana Sánchez-Wandelmer, Franziska Kriegenburg, 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*

*Corresponding author voor dit werk

OnderzoeksoutputAcademicpeer review

61 Citaten (Scopus)
285 Downloads (Pure)


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

Originele taal-2English
Aantal pagina's10
TijdschriftNature Communications
StatusPublished - 18-aug.-2017


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