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A more recent version of this article appeared on February 1, 2007 Originally published as MBC in Press, 10.1091/mbc.E06-07-0612 on December 4, 2006
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Submitted on July 19, 2006
Revised on November 1, 2006
Accepted on November 21, 2006
Life Sciences Institute, and Departments of Molecular, Cellular, and Developmental Biology and Biological Chemistry, University of Michigan, Ann Arbor, MI 48109
Monitoring Editor: Suresh Subramani
Autophagy is a conserved degradative pathway that is induced in response to various stress and developmental conditions in eukaryotic cells. It allows the elimination of cytosolic proteins and organelles in the lysosome/vacuole. In the yeast S. cerevisiae, the integral membrane protein Atg9 cycles between mitochondria and the pre-autophagosomal structure (PAS), the nucleating site for formation of the sequestering vesicle, suggesting a role in supplying membrane for vesicle formation and/or expansion during autophagy. To better understand the mechanisms involved in Atg9 cycling, we performed a yeast two-hybrid-based screen and identified a peripheral membrane protein, Atg11, which interacts with Atg9. We show that Atg11 governs Atg9 cycling through the PAS during specific autophagy. We also demonstrate that the integrity of the actin cytoskeleton is essential for correct targeting of Atg11 to the PAS. We propose that a pool of Atg11 mediates anterograde transport of Atg9 to the PAS dependent on the actin cytoskeleton during yeast vegetative growth.
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