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

Rao, Y., Perna, M. G., Hofmann, B., Beier, V., & Wollert, T. (2016). The Atg1-kinase complex tethers Atg9-vesicles to initiate autophagy. NATURE COMMUNICATIONS, 7: 10338. doi:10.1038/ncomms10338.

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 Creators:
Rao, Yijian1, Author              
Perna, Marco G.1, Author              
Hofmann, Benjamin1, Author              
Beier, Viola1, Author              
Wollert, Thomas1, Author              
Affiliations:
1Wollert, Thomas / Molecular Membrane and Organelle Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565175              

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Free keywords: PROTEIN-KINASE COMPLEX; SACCHAROMYCES-CEREVISIAE; CIRCULAR-DICHROISM; RECRUITS ATG9; EARLY STEPS; BIOGENESIS; MACHINERY; TOR; ATG17-ATG31-ATG29; PHOSPHORYLATION
 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.

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Language(s): eng - English
 Dates: 2016
 Publication Status: Published online
 Pages: 13
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000369021900002
DOI: 10.1038/ncomms10338
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Title: NATURE COMMUNICATIONS
Source Genre: Journal
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Publ. Info: MACMILLAN BUILDING, 4 CRINAN ST, LONDON N1 9XW, ENGLAND : NATURE PUBLISHING GROUP
Pages: - Volume / Issue: 7 Sequence Number: 10338 Start / End Page: - Identifier: ISSN: 2041-1723