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¹ Department of Molecular, Cellular, and Developmental Biology, ² Department of Biological Chemistry, and ³ Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109

Correspondence to Daniel J. Klionsky: klionsky{at}umich.edu

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 Saccharomyces cerevisiae, the integral membrane protein Atg9 (autophagy-related protein 9) cycles between mitochondria and the preautophagosomal 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, that 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 the anterograde transport of Atg9 to the PAS that is dependent on the actin cytoskeleton during yeast vegetative growth.

Abbreviations used in this paper: AD, activation domain; Ape1, aminopeptidase I; Atg, autophagy related; BD, binding domain; BFP, blue fluorescent protein; CC, coiled coil; Cvt, cytoplasm to vacuole targeting; PA, protein A; PAS, preautophagosomal structure; prApe1, precursor form of Ape1; SMD, synthetic minimal medium.

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