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Vol. 16, Issue 5, 2544-2553, May 2005
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* Division of Molecular Cell Biology, National Institute for Basic Biology, Okazaki 444-8585, Japan;
School of Life Science, The Graduate University for Advance Studies, Okazaki 444-8585, Japan;
CREST, Japan Science and Technology Agency, Kawaguchi 332-0012, Japan; and
Department of Biosystems Science, Graduate School of Science and Technology, Kobe University, Kobe 657-8501, Japan
Submitted August 6, 2004;
Accepted February 18, 2005
Monitoring Editor: Suresh Subramani
In eukaryotic cells, nutrient starvation induces the bulk degradation of cellular materials; this process is called autophagy. In the yeast Saccharomyces 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
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 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.
Abbreviations used: ALP, alkaline phosphatase (Pho8); ATG genes, autophagy-related genes; Cvt, cytoplasm to vacuole targeting; HA, hemagglutinin.
Address correspondence to: Yoshinori Ohsumi (yohsumi{at}nibb.ac.jp).
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