Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth

Research output: Contribution to journalJournal articleResearchpeer-review

  • Philipp Wild
  • Hesso Farhan
  • David G McEwan
  • Sebastian Wagner
  • Vladimir V Rogov
  • Nathan R Brady
  • Benjamin Richter
  • Jelena Korac
  • Oliver Waidmann
  • Choudhary, Chuna Ram
  • Volker Dötsch
  • Dirk Bumann
  • Ivan Dikic
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.
Original languageEnglish
Issue number6039
Pages (from-to)228-33
Number of pages6
Publication statusPublished - 8 Jul 2011

ID: 33753972