title: Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth.
abstract: 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.
authors: Frankfurt Institute for Molecular Life Sciences and Institute of Biochemistry II, Goethe University School of Medicine, Frankfurt (Main), Germany.
authors: Philipp
authors: P
authors: Wild
authors: Hesso
authors: H
authors: Farhan
authors: David G
authors: DG
authors: McEwan
authors: Sebastian
authors: S
authors: Wagner
authors: Vladimir V
authors: VV
authors: Rogov
authors: Nathan R
authors: NR
authors: Brady
authors: Benjamin
authors: B
authors: Richter
authors: Jelena
authors: J
authors: Korac
authors: Oliver
authors: O
authors: Waidmann
authors: Chunaram
authors: C
authors: Choudhary
authors: Volker
authors: V
authors: Dötsch
authors: Dirk
authors: D
authors: Bumann
authors: Ivan
authors: I
authors: Dikic
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