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MBC in Press, published online ahead of print February 20, 2008
Mol. Biol. Cell 10.1091/mbc.E07-10-1048

A more recent version of this article appeared on May 1, 2008
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Submitted on October 18, 2007
Revised on February 7, 2008
Accepted on February 13, 2008

Organization of the Pre-Autophagosomal Structure Responsible for Autophagosome Formation

Tomoko Kawamata,*{dagger} Yoshiaki Kamada,* Yukiko Kabeya, Takayuki Sekito, and Yoshinori Ohsumi

Department of Cell Biology, National Institute for Basic Biology, Okazaki 444-8585, Japan; School of Life Science, The Graduate University for Advanced Studies, Okazaki 444-8585, Japan

Monitoring Editor: Suresh Subramani

Autophagy induced by nutrient depletion is involved in survival during starvation conditions. In addition to starvation-induced autophagy, the yeast S. cerevisiae also has a constitutive autophagy-like system, the Cvt pathway. Among 31 Atg (autophagy-related) proteins, the function of Atg17, Atg29, and Atg31 are required specifically for autophagy. In this study, we investigated the role of autophagy–specific (i.e., nonCvt) proteins under autophagy-inducing conditions. For this purpose, we used atg11{Delta} cells in which the Cvt pathway is abrogated. The autophagy-unique proteins are required for the localization of Atg proteins to the pre-autophagosomal structure (PAS), the putative site for autophagosome formation, under starvation condition. It is likely that these Atg proteins function as a ternary complex, because Atg29 and Atg31 bind to Atg17. The Atg1 kinase complex (Atg1-Atg13) is also essential for recruitment of Atg proteins to the PAS. The assembly of Atg proteins to the PAS is observed only under autophagy-inducing conditions, indicating that this structure is specifically involved in autophagosome formation. Our results suggest that Atg1 complex and the autophagy-unique Atg proteins cooperatively organize the PAS in response to starvation signals.

*These authors contributed equally to this work.

{dagger}Present address: Institute of Molecular and Cellular Biosciences, The University of Tokyo, Tokyo 113-0032, Japan.

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




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