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Abstract
TBK1 phosphorylates WIPI2 at Ser96, enhancing its role in autophagosome formation during Salmonella Typhimurium infection.
- WIPI2 is identified as a novel phosphorylation target of TBK1 in the context of bacterial infection.
- Phosphorylation at Ser96 increases WIPI2's interaction with ATG16L1 and its binding to PtdIns3P.
- The localization of WIPI2 to bacteria is dependent on its interaction with ATG16L1 associated with the Salmonella-containing vacuole.
- TBK1-mediated phosphorylation of WIPI2 is necessary for effective bacterial clearance.
- The study suggests a mechanism linking bacterial recognition with the assembly of autophagosomes.
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