Journal
MOLECULAR CELL
Volume 43, Issue 4, Pages 572-585Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2011.06.018
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Funding
- National Institutes of Health [HL084199, CA123777, CA076379, DK074519, GM097057, CA099179]
- NINDS
- Burroughs Welcome Fund
- American Society of Hematology
- American Diabetes Association [ADA 7-07-CD-08]
- monies from the State of Florida
- monies from the American Lebanese Syrian Associated Charities (ALSAC)
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Autophagy, the primary recycling pathway of cells, plays a critical role in mitochondrial quality control under normal growth conditions and in the response to cellular stress. The Hsp90-Cdc37 chaperone complex coordinately regulates the activity of select kinases to orchestrate many facets of the stress response. Although both maintain mitochondrial integrity, the relationship between Hsp90-Cdc37 and autophagy has not been well characterized. Ulk1, one of the mammalian homologs of yeast Atg1, is a serine-threonine kinase required for mitophagy. Here we show that the interaction between Ulk1 and Hsp90-Cdc37 stabilizes and activates Ulk1, which in turn is required for the phosphorylation and release of Atg13 from Ulk1, and for the recruitment of Atg13 to damaged mitochondria. Hsp90-Cdc37, Ulk1, and Atg13 phosphorylation are all required for efficient mitochondrial clearance. These findings establish a direct pathway that integrates Ulk1- and Atg13-directed mitophagy with the stress response coordinated by Hsp90 and Cdc37.
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