Solution structure of the Atg1 complex: Implications for the architecture of the phagophore assembly site

Jürgen Köfinger, Michael J. Ragusa, Il Hyung Lee, Gerhard Hummer, James H. Hurley

Research output: Contribution to journalArticlepeer-review

27 Scopus citations

Abstract

The biogenesis of autophagosomes commences at the phagophore assembly site (PAS), a protein-vesicle ultrastructure that is organized by the Atg1 complex. The Atg1 complex consists of the Atg1 protein kinase, the intrinsically disordered region-rich Atg13, and the dimeric double crescent-shaped Atg17-Atg31-Atg29 subcomplex. We show that the PAS contains a relatively uniform ∼28 copies of Atg17, and upon autophagy induction, similar numbers of Atg1 and Atg13 molecules. We then apply ensemble refinement of small-angle X-ray scattering to determine the solution structures of the Atg1-Atg13 and Atg17-Atg31-Atg29 subcomplexes and the Atg1 complex, using a trimmed minipentamer tractable to biophysical studies. We observe tetramers of Atg1 pentamers that assemble via Atg17-Atg31-Atg29. This leads to a model for the higher organization of the Atg1 complex in PAS scaffolding.

Original languageEnglish
Pages (from-to)809-818
Number of pages10
JournalStructure
Volume23
Issue number5
DOIs
StatePublished - 5 May 2015

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