Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth
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Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth. / Wild, Philipp; Farhan, Hesso; McEwan, David G; Wagner, Sebastian; Rogov, Vladimir V; Brady, Nathan R; Richter, Benjamin; Korac, Jelena; Waidmann, Oliver; Choudhary, Chunaram; Dötsch, Volker; Bumann, Dirk; Dikic, Ivan.
In: Science, Vol. 333, No. 6039, 08.07.2011, p. 228-33.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth
AU - Wild, Philipp
AU - Farhan, Hesso
AU - McEwan, David G
AU - Wagner, Sebastian
AU - Rogov, Vladimir V
AU - Brady, Nathan R
AU - Richter, Benjamin
AU - Korac, Jelena
AU - Waidmann, Oliver
AU - Choudhary, Chunaram
AU - Dötsch, Volker
AU - Bumann, Dirk
AU - Dikic, Ivan
PY - 2011/7/8
Y1 - 2011/7/8
N2 - 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.
AB - 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.
U2 - 10.1126/science.1205405
DO - 10.1126/science.1205405
M3 - Journal article
C2 - 21617041
VL - 333
SP - 228
EP - 233
JO - Science
JF - Science
SN - 0036-8075
IS - 6039
ER -
ID: 33753972