Phosphorylation of ULK1 affects autophagosome fusion and links chaperone-mediated autophagy to macroautophagy
作者： Chenyao Wang , Huafei Wang , Deyi Zhang , Wenwen Luo , Ruilong Liu
DOI: 10.1038/S41467-018-05449-1
关键词:
摘要: The Unc-51 like autophagy activating kinase 1 (ULK1) complex plays a central role in the initiation stage of autophagy. However, function ULK1 late is unknown. Here, we report that ULK1, involved initiation, promotes autophagosome–lysosome fusion. PKCα phosphorylates and prevents autolysosome formation. phosphorylation does not change its activity; however, it decreases fusion by reducing affinity for syntaxin 17 (STX17). Unphosphorylated recruited STX17 increased STX17′s towards synaptosomal-associated protein 29 (SNAP29). Additionally, enhances interaction with heat shock cognate 70 kDa (HSC70) increases degradation through chaperone-mediated (CMA). Our study unearths key mechanism underlying formation, process which activity an instrumental role, reveals significance mutual regulation macroautophagy CMA maintaining balance ULK well-known initiating autophagy, to recycle cellular components response nutritional stress. authors demonstrate auotophagosome–lysosome provide direct link between chaperone mediated
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