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The Atg1–kinase complex tethers Atg9-vesicles to initiate autophagy

Author

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  • Yijian Rao

    (Molecular Membrane and Organelle Biology, Max Planck Institute of Biochemistry)

  • Marco G. Perna

    (Molecular Membrane and Organelle Biology, Max Planck Institute of Biochemistry)

  • Benjamin Hofmann

    (Molecular Membrane and Organelle Biology, Max Planck Institute of Biochemistry)

  • Viola Beier

    (Molecular Membrane and Organelle Biology, Max Planck Institute of Biochemistry)

  • Thomas Wollert

    (Molecular Membrane and Organelle Biology, Max Planck Institute of Biochemistry)

Abstract

Autophagosomes are double-membrane vesicles that sequester cytoplasmic material for lysosomal degradation. Their biogenesis is initiated by recruitment of Atg9-vesicles to the phagophore assembly site. This process depends on the regulated activation of the Atg1–kinase complex. However, the underlying molecular mechanism remains unclear. Here we reconstitute this early step in autophagy from purified components in vitro. We find that on assembly from its cytoplasmic subcomplexes, the Atg1–kinase complex becomes activated, enabling it to recruit and tether Atg9-vesicles. The scaffolding protein Atg17 targets the Atg1–kinase complex to autophagic membranes by specifically recognizing the membrane protein Atg9. This interaction is inhibited by the two regulatory subunits Atg31 and Atg29. Engagement of the Atg1–Atg13 subcomplex restores the Atg9-binding and membrane-tethering activity of Atg17. Our data help to unravel the mechanism that controls Atg17-mediated tethering of Atg9-vesicles, providing the molecular basis to understand initiation of autophagosome-biogenesis.

Suggested Citation

  • Yijian Rao & Marco G. Perna & Benjamin Hofmann & Viola Beier & Thomas Wollert, 2016. "The Atg1–kinase complex tethers Atg9-vesicles to initiate autophagy," Nature Communications, Nature, vol. 7(1), pages 1-13, April.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms10338
    DOI: 10.1038/ncomms10338
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    Cited by:

    1. Keisuke Tabata & Kenta Imai & Koki Fukuda & Kentaro Yamamoto & Hayato Kunugi & Toshiharu Fujita & Tatsuya Kaminishi & Christian Tischer & Beate Neumann & Sabine Reither & Fatima Verissimo & Rainer Pep, 2024. "Palmitoylation of ULK1 by ZDHHC13 plays a crucial role in autophagy," Nature Communications, Nature, vol. 15(1), pages 1-15, December.

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