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Vol. 19, Issue 8, 3290-3298, August 2008

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Atg8 Controls Phagophore Expansion during Autophagosome Formation

Zhiping Xie^*, Usha Nair^*, and Daniel J. Klionsky^*,

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

Submitted January 2, 2008; Revised April 21, 2008; Accepted May 16, 2008
Monitoring Editor: Howard Riezman

InCytes from MBC

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. On the basis of the dynamics of Atg8, we present a multistage 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)

Abbreviations used: ALP, alkaline phosphatase; Atg, autophagy-related; Cvt, cytoplasm to vacuole targeting; GFP, green fluorescent protein; prApe1, precursor aminopeptidase I.

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