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Solution Structure of the Atg1 Complex: Implications for the Architecture of the Phagophore Assembly Site

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Köfinger,  Jürgen
Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society;

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Hummer,  Gerhard
Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Köfinger, J., Ragusa, M. J., Lee, I.-H., Hummer, G., & Hurley, J. H. (2015). Solution Structure of the Atg1 Complex: Implications for the Architecture of the Phagophore Assembly Site. Structure, 23(5), 809-818. doi:10.1016/j.str.2015.02.012.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002A-4829-1
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.