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

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.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-002A-4829-1 Version Permalink: https://hdl.handle.net/21.11116/0000-000B-A9E3-6
Genre: Journal Article

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 Creators:
Köfinger, Jürgen1, Author                 
Ragusa, Michael J.2, Author
Lee, Il-Hyung2, Author
Hummer, Gerhard1, Author                 
Hurley, James H.2, 3, Author
Affiliations:
1Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society, ou_2068292              
2Department of Molecular and Cell Biology, California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720, USA, ou_persistent22              
3Life Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA, ou_persistent22              

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 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.

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Language(s): eng - English
 Dates: 2014-12-122015-02-242015-03-262015-05-05
 Publication Status: Issued
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.str.2015.02.012
 Degree: -

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Title: Structure
  Other : Structure
Source Genre: Journal
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Publ. Info: London : Cell Press
Pages: - Volume / Issue: 23 (5) Sequence Number: - Start / End Page: 809 - 818 Identifier: ISSN: 0969-2126
CoNE: https://pure.mpg.de/cone/journals/resource/954927002244_1