The Intrinsically Disordered Protein Atg13 Mediates Supramolecular Assembly of Autophagy Initiation Complexes

Autophagosome formation in yeast entails starvation-induced assembly of the pre-autophagosomal structure (PAS), in which multiple Atg1 complexes (composed of Atg1, Atg13, and the Atg17-Atg29-Atg31 subcomplex) are initially engaged. However, the molecular mechanisms underlying the multimeric assembly...

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Vydané v:	Developmental cell Ročník 38; číslo 1; s. 86 - 99
Hlavní autori:	Yamamoto, Hayashi, Fujioka, Yuko, Suzuki, Sho W, Noshiro, Daisuke, Suzuki, Hironori, Kondo-Kakuta, Chika, Kimura, Yayoi, Hirano, Hisashi, Ando, Toshio, Noda, Nobuo N, Ohsumi, Yoshinori
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	United States 11.07.2016
Predmet:	Adaptor Proteins, Signal Transducing - chemistry Adaptor Proteins, Signal Transducing - genetics Adaptor Proteins, Signal Transducing - metabolism Amino Acid Sequence Autophagy Autophagy-Related Proteins - chemistry Autophagy-Related Proteins - genetics Autophagy-Related Proteins - metabolism Intrinsically Disordered Proteins - chemistry Intrinsically Disordered Proteins - genetics Intrinsically Disordered Proteins - metabolism Membrane Proteins - chemistry Membrane Proteins - genetics Membrane Proteins - metabolism Multiprotein Complexes - chemistry Multiprotein Complexes - genetics Multiprotein Complexes - metabolism Phagosomes - physiology Phosphorylation Protein Binding Protein Conformation Protein Kinases - chemistry Protein Kinases - genetics Protein Kinases - metabolism Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - growth & development Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Sequence Homology, Amino Acid
ISSN:	1878-1551
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Shrnutí:	Autophagosome formation in yeast entails starvation-induced assembly of the pre-autophagosomal structure (PAS), in which multiple Atg1 complexes (composed of Atg1, Atg13, and the Atg17-Atg29-Atg31 subcomplex) are initially engaged. However, the molecular mechanisms underlying the multimeric assembly of these complexes remain unclear. Using structural and biological techniques, we herein demonstrate that Atg13 has a large intrinsically disordered region (IDR) and interacts with two distinct Atg17 molecules using two binding regions in the IDR. We further reveal that these two binding regions are essential not only for Atg1 complex assembly in vitro, but also for PAS organization in vivo. These findings underscore the structural and functional significance of the IDR of Atg13 in autophagy initiation: Atg13 provides intercomplex linkages between Atg17-Atg29-Atg31 complexes, thereby leading to supramolecular self-assembly of Atg1 complexes, in turn accelerating the initial events of autophagy, including autophosphorylation of Atg1, recruitment of Atg9 vesicles, and phosphorylation of Atg9 by Atg1.
Bibliografia:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1878-1551
DOI:	10.1016/j.devcel.2016.06.015