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Phosphorylation-Dependent Feedback Inhibition of RIG-I by DAPK1 Identified by Kinome-wide siRNA Screening

J. Willemsen, O. Wicht, JC. Wolanski, N. Baur, S. Bastian, DA. Haas, P. Matula, B. Knapp, L. Meyniel-Schicklin, C. Wang, R. Bartenschlager, V. Lohmann, K. Rohr, H. Erfle, L. Kaderali, J. Marcotrigiano, A. Pichlmair, M. Binder,

. 2017 ; 65 (3) : 403-415.e8. [pub] 20170126

Jazyk angličtina Země Spojené státy americké

Typ dokumentu časopisecké články

Perzistentní odkaz   https://www.medvik.cz/link/bmc17031082

Cell-autonomous induction of type I interferon must be stringently regulated. Rapid induction is key to control virus infection, whereas proper limitation of signaling is essential to prevent immunopathology and autoimmune disease. Using unbiased kinome-wide RNAi screening followed by thorough validation, we identified 22 factors that regulate RIG-I/IRF3 signaling activity. We describe a negative-feedback mechanism targeting RIG-I activity, which is mediated by death associated protein kinase 1 (DAPK1). RIG-I signaling triggers DAPK1 kinase activation, and active DAPK1 potently inhibits RIG-I stimulated IRF3 activity and interferon-beta production. DAPK1 phosphorylates RIG-I in vitro at previously reported as well as other sites that limit 5'ppp-dsRNA sensing and virtually abrogate RIG-I activation.

Citace poskytuje Crossref.org

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