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 and Fulvio Reggiori ()
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Jana Sánchez-Wandelmer: University of Groningen, University Medical Center Groningen
Franziska Kriegenburg: University of Groningen, University Medical Center Groningen
Sabrina Rohringer: University of Vienna
Martina Schuschnig: University of Vienna
Rubén Gómez-Sánchez: University of Groningen, University Medical Center Groningen
Bettina Zens: University of Vienna
Susana Abreu: University of Groningen, University Medical Center Groningen
Ralph Hardenberg: University of Groningen, University Medical Center Groningen
David Hollenstein: University of Vienna
Jieqiong Gao: University of Osnabrück, Department of Biology/Chemistry, Biochemistry section
Christian Ungermann: University of Osnabrück, Department of Biology/Chemistry, Biochemistry section
Sascha Martens: University of Vienna
Claudine Kraft: University of Vienna
Fulvio Reggiori: University of Groningen, University Medical Center Groningen

Nature Communications, 2017, vol. 8, issue 1, 1-10

Abstract: Abstract 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.

Date: 2017
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DOI: 10.1038/s41467-017-00302-3

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