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MBC in Press, published online ahead of print May 18, 2005
Mol. Biol. Cell 10.1091/mbc.E04-10-0894

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Submitted on October 13, 2004
Revised on March 17, 2005
Accepted on May 5, 2005

Atg17 Regulates the Magnitude of the Autophagic Response

Heesun Cheong, Tomohiro Yorimitsu, Fulvio Reggiori, Julie E. Legakis, Chao-Wen Wang, and Daniel J. Klionsky

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

Monitoring Editor: Randy Schekman

Autophagy is a catabolic process used by eukaryotic cells for the degradation and recycling of cytosolic proteins and excess or defective organelles. In yeast, autophagy is primarily a response to nutrient limitation while in higher eukaryotes it also plays a role in developmental processes. Due to its essentially unlimited degradative capacity, it is critical that regulatory mechanisms are in place to modulate the timing and magnitude of the autophagic response. One set of proteins that appears to function in this regard includes a complex that contains the Atg1 kinase. Aside from Atg1, the proteins in this complex participate primarily in either nonspecific autophagy or specific types of autophagy, including the cytoplasm to vacuole targeting pathway, which operates under vegetative growth conditions, and peroxisome degradation. Accordingly, these proteins are prime candidates for factors that regulate the conversion between these pathways, including the change in size of the sequestering vesicle, the most obvious morphological difference. The atg17{Delta} mutant forms a reduced number of small autophagosomes. As a result, it is defective in peroxisome degradation, and is partially defective for autophagy. Atg17 interacts with both Atg1 and Atg13, via two coiled-coil domains, and these interactions facilitate its inclusion in the Atg1 complex.


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




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