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MBC in Press, published online ahead of print May 28, 2008
Mol. Biol. Cell 10.1091/mbc.E07-12-1292

A more recent version of this article appeared on August 1, 2008
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Submitted on January 2, 2008
Revised on April 21, 2008
Accepted on May 16, 2008

Atg8 Controls Phagophore Expansion during Autophagosome Formation

Zhiping Xie,* Usha Nair,* and Daniel J. Klionsky*{dagger}

*Life Sciences Institute and Department of Molecular, Cellular and Developmental Biology, and {dagger}Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109

Monitoring Editor: Howard Riezman

Autophagy is a potent intracellular degradation process with pivotal roles in health and disease. Atg8, a lipid conjugated ubiquitin-like protein, is required for the formation of autophagosomes, double-membrane vesicles responsible for the delivery of cytoplasmic material to lysosomes. How and when Atg8 functions in this process, however, is not clear. Here we show that Atg8 controls the expansion of the autophagosome precursor, the phagophore, and give the first real-time, observation-based temporal dissection of the autophagosome formation process. We demonstrate that the amount of Atg8 determines the size of autophagosomes. During autophagosome biogenesis, Atg8 forms an expanding structure and later dissociates from the site of vesicle formation. Based on the dynamics of Atg8, we present a multi-stage model of autophagosome formation. This model provides a foundation for future analyses of the functions and dynamics of known autophagy-related proteins and for screening new genes.

Address correspondence to: Daniel J. Klionsky (klionsky{at}umich.edu)




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