期刊
SCIENCE
卷 333, 期 6039, 页码 228-233出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1205405
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资金
- Deutsche Forschungsgemeinschaft
- Goethe University Frankfurt [EXC115]
- Landes-Offensive zur Entwicklung Wissentschaftlich-okonomischer Exzellenz
- European Research Council (ERC) under the European Union [250241-LineUb]
- Swiss National Fonds [3100A0-121834/1]
- Novo Nordisk Foundation
- Split, Croatia, government
- Danish Council for Independent Research [FSS: 10-085134]
- Helmholtz Association
- Swiss National Science Foundation [31003A-121834]
- Swiss National Science Foundation (SNF) [31003A-121834] Funding Source: Swiss National Science Foundation (SNF)
- Novo Nordisk Foundation Center for Protein Research [PI Chunaram Choudhary] Funding Source: researchfish
Selective autophagy can be mediated via receptor molecules that link specific cargoes to the autophagosomal membranes decorated by ubiquitin-like microtubule-associated protein light chain 3 (LC3) modifiers. Although several autophagy receptors have been identified, little is known about mechanisms controlling their functions in vivo. In this work, we found that phosphorylation of an autophagy receptor, optineurin, promoted selective autophagy of ubiquitin-coated cytosolic Salmonella enterica. The protein kinase TANK binding kinase 1 (TBK1) phosphorylated optineurin on serine-177, enhancing LC3 binding affinity and autophagic clearance of cytosolic Salmonella. Conversely, ubiquitin-or LC3-binding optineurin mutants and silencing of optineurin or TBK1 impaired Salmonella autophagy, resulting in increased intracellular bacterial proliferation. We propose that phosphorylation of autophagy receptors might be a general mechanism for regulation of cargo-selective autophagy.
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