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Atg17 recruits Atg9 to organize the pre‐autophagosomal structure
Author(s) -
Sekito Takayuki,
Kawamata Tomoko,
Ichikawa Rie,
Suzuki Kuninori,
Ohsumi Yoshinori
Publication year - 2009
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1111/j.1365-2443.2009.01299.x
Subject(s) - autophagy , microbiology and biotechnology , biology , cytoplasm , vacuole , organelle , biochemistry , apoptosis
Autophagy is a degradation system of cytoplasmic proteins and organelles via formation of double‐membrane vesicles called autophagosomes. In the yeast Saccharomyces cerevisiae , autophagosomes are formed via the pre‐autophagosomal structure (PAS) in a manner dependent on Atg proteins. Under nutrient‐rich condition, Atg9 is recruited to the PAS by binding to Atg11 for the Cvt pathway. However, because Atg9 is recruited to the PAS in atg11 Δ cells in starved condition and autophagy is induced, autophagy‐specific mechanism for the Atg9 recruitment to the PAS has been assumed. Here, we demonstrate that, in autophagy‐inducing condition, Atg9 is recruited to the PAS in a manner dependent on Atg17. Atg9 physically interacts with Atg17 in the presence of rapamycin. This interaction requires Atg1, a protein kinase essential for autophagy. Consistently, the Atg17‐dependent PAS localization of Atg9 requires Atg1. However, its kinase activity is dispensable for this process. It rather regulates the equilibrium of assembly and disassembly of Atg9 at the PAS.