期刊
NATURE CELL BIOLOGY
卷 15, 期 7, 页码 741-+出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncb2757
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资金
- UCSD Neuroscience Microscopy Shared Facility [P30 NS047101]
- National Institutes of Health (NIH) [GM51586, GM62694, CA108941]
- Department of Defense [W81XWH-0901-0279]
- Canadian Institutes of Health Research (CIHR) postdoctoral fellowship
Autophagy is the primary cellular catabolic program activated in response to nutrient starvation. Initiation of autophagy, particularly by amino-acid withdrawal, requires the ULK kinases. Despite its pivotal role in autophagy initiation, little is known about the mechanisms by which ULK promotes autophagy. Here we describe a molecular mechanism linking ULK to the pro-autophagic lipid kinase VPS34. Following amino-acid starvation or mTOR inhibition, the activated ULK1 phosphorylates Beclin-1 on Ser 14, thereby enhancing the activity of the ATG14L-containing VPS34 complexes. The Beclin-1 Ser 14 phosphorylation by ULK is required for full autophagic induction in mammals and this requirement is conserved in Caenorhabditis elegans. Our study reveals a molecular link from ULK1 to activation of the autophagy-specific VPS34 complex and autophagy induction.
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