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MBC in Press, published online ahead of print March 2, 2005
Mol. Biol. Cell 10.1091/mbc.E04-08-0669

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Submitted on August 6, 2004
Accepted on February 18, 2005

Atg17 Functions in Cooperation with Atg1 and Atg13 in Yeast Autophagy

Yukiko Kabeya,* Yoshiaki Kamada,*{dagger}{ddagger} Misuzu Baba,* Hirosato Takikawa,{sect} Mitsuru Sasaki,{sect} and Yoshinori Ohsumi*{dagger}

*Division of Molecular Cell Biology, National Institute for Basic Biology, Okazaki 444-8585, Japan; {dagger}School of Life Science, The Graduate University for Advance Studies, Okazaki 444-8585, Japan; {ddagger}CREST, Japan Science and Technology Agency, Kawaguchi 332-0012, Japan; {sect}Department of Biosystems Science, Graduate School of Science and Technology, Kobe University, Kobe 657-8501, Japan

Monitoring Editor: Suresh Subramani

In eukaryotic cells, nutrient starvation induces the bulk degradation of cellular materials; this process is called autophagy. In the yeast S. cerevisiae, most of the ATG (AuTophaGy) genes are involved in not only the process of degradative autophagy, but also a biosynthetic process, the cytoplasm to vacuole (Cvt) pathway. In contrast, the ATG17 gene is required specifically in autophagy. To better understand the function of Atg17, we have performed a biochemical characterization of the Atg17 protein. We found that the atg17{Delta} mutant under starvation condition was largely impaired in autophagosome formation and only rarely contained small autophagosomes, whose size was less than one-half of normal autophagosomes in diameter. Two-hybrid analyses and coimmunoprecipitation experiments demonstrated that Atg17 physically associates with Atg1-Atg13 complex, and this binding was enhanced under starvation conditions. Atg17-Atg1 binding was not detected in atg13{Delta} mutant cells, suggesting that Atg17 interacts with Atg1 through Atg13. A point mutant of Atg17, Atg17C24R, showed reduced affinity for Atg13, resulting in impaired Atg1 kinase activity and significant defects in autophagy. Taken together, these results indicate that Atg17-Atg13 complex formation plays an important role in normal autophagosome formation via binding to and activating the Atg1 kinase.

Address correspondence to: Yoshinori Ohsumi (yohsumi{at}nibb.ac.jp)




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