期刊
MOLECULAR CELL
卷 53, 期 3, 页码 471-483出版社
CELL PRESS
DOI: 10.1016/j.molcel.2013.12.011
关键词
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资金
- Austrian Science Fund [FWF W1220-B09, FWF P 25522-B20]
- FEMtech Praktikum by the Federal Ministry for Transport, Innovation and Technology
- European Research Council
- SystemsX.ch
- Swiss National Science Foundation
- ETH Zurich
- EU
- EMBO long-term fellowship
- Vienna Research Groups for Young Investigators grant from the Vienna Science and Technology Fund [WWTF VRG10-001]
- National Institutes of Health [R01 GM105947]
- Austrian Science Fund (FWF) [P 25522] Funding Source: researchfish
- Austrian Science Fund (FWF) [P25522] Funding Source: Austrian Science Fund (FWF)
Bulk degradation of cytoplasmic material is mediated by a highly conserved intracellular trafficking pathway termed autophagy. This pathway is characterized by the formation of double-membrane vesicles termed autophagosomes engulfing the substrate and transporting it to the vacuole/lysosorne for breakdown and recycling. The Atg1/ULK1 kinase is essential for this process; however, little is known about its targets and the means by which it controls autophagy. Here we have screened for Atg1 kinase substrates using consensus peptide arrays and identified three components of the autophagy machinery. The multimembrane-spanning protein Atg9 is a direct target of this kinase essential for autophagy. Phosphorylated Atg9 is then required for the efficient recruitment of Atg8 and Atg18 to the site of autophagosome formation and subsequent expansion of the isolation membrane, a prerequisite for a functioning autophagy pathway. These findings show that the Atg1 kinase acts early in autophagy by regulating the outgrowth of autophagosomal membranes.
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