Autophagy initiation by ULK complex assembly on ER tubulovesicular regions marked by ATG9 vesicles

Eleftherios Karanasios, Simon A. Walker, Hanneke Okkenhaug, Maria Manifava, Eric Hummel, Hans Zimmermann, Qashif Ahmed, Marie-Charlotte Domart, Lucy Collinson and Nicholas T. Ktistakis ()
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Eleftherios Karanasios: Signalling Programme, The Babraham Institute
Simon A. Walker: Signalling Programme, The Babraham Institute
Hanneke Okkenhaug: Signalling Programme, The Babraham Institute
Maria Manifava: Signalling Programme, The Babraham Institute
Eric Hummel: Carl Zeiss Microscopy GmbH
Hans Zimmermann: Carl Zeiss Microscopy GmbH
Qashif Ahmed: Signalling Programme, The Babraham Institute
Marie-Charlotte Domart: The Francis Crick Institute
Lucy Collinson: The Francis Crick Institute
Nicholas T. Ktistakis: Signalling Programme, The Babraham Institute

Nature Communications, 2016, vol. 7, issue 1, 1-17

Abstract: Abstract Autophagosome formation requires sequential translocation of autophagy-specific proteins to membranes enriched in PI3P and connected to the ER. Preceding this, the earliest autophagy-specific structure forming de novo is a small punctum of the ULK1 complex. The provenance of this structure and its mode of formation are unknown. We show that the ULK1 structure emerges from regions, where ATG9 vesicles align with the ER and its formation requires ER exit and coatomer function. Super-resolution microscopy reveals that the ULK1 compartment consists of regularly assembled punctate elements that cluster in progressively larger spherical structures and associates uniquely with the early autophagy machinery. Correlative electron microscopy after live imaging shows tubulovesicular membranes present at the locus of this structure. We propose that the nucleation of autophagosomes occurs in regions, where the ULK1 complex coalesces with ER and the ATG9 compartment.

Date: 2016
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DOI: 10.1038/ncomms12420

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