Hsp90-Cdc37 Chaperone Complex Regulates Ulk1- and Atg13-Mediated Mitophagy
作者： Joung Hyuck Joo , Frank C Dorsey , Aashish Joshi , Kristin M Hennessy-Walters , Kristie L Rose
DOI: 10.1016/J.MOLCEL.2011.06.018
关键词:
摘要: Autophagy, the primary recycling pathway of cells, plays a critical role in mitochondrial quality control under normal growth conditions and response to cellular stress. The Hsp90-Cdc37 chaperone complex coordinately regulates activity select kinases orchestrate many facets stress response. Although both maintain integrity, relationship between autophagy has not been well characterized. Ulk1, one mammalian homologs yeast Atg1, is serine-threonine kinase required for mitophagy. Here we show that interaction Ulk1 stabilizes activates which turn phosphorylation release Atg13 from recruitment damaged mitochondria. Hsp90-Cdc37, are all efficient clearance. These findings establish direct integrates Ulk1- Atg13-directed mitophagy with coordinated by Hsp90 Cdc37.
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