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Atg4 proteolytic activity can be inhibited by Atg1 phosphorylation

Author

Listed:
  • Jana Sánchez-Wandelmer

    (University of Groningen, University Medical Center Groningen
    University Medical Center Utrecht)

  • Franziska Kriegenburg

    (University of Groningen, University Medical Center Groningen
    University Medical Center Utrecht)

  • Sabrina Rohringer

    (University of Vienna)

  • Martina Schuschnig

    (University of Vienna)

  • Rubén Gómez-Sánchez

    (University of Groningen, University Medical Center Groningen
    University Medical Center Utrecht)

  • Bettina Zens

    (University of Vienna)

  • Susana Abreu

    (University of Groningen, University Medical Center Groningen
    University Medical Center Utrecht)

  • 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
    University Medical Center Utrecht)

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.

Suggested Citation

  • Jana Sánchez-Wandelmer & Franziska Kriegenburg & Sabrina Rohringer & Martina Schuschnig & Rubén Gómez-Sánchez & Bettina Zens & Susana Abreu & Ralph Hardenberg & David Hollenstein & Jieqiong Gao & Chri, 2017. "Atg4 proteolytic activity can be inhibited by Atg1 phosphorylation," Nature Communications, Nature, vol. 8(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-00302-3
    DOI: 10.1038/s41467-017-00302-3
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