DAI/ZBP1 recruits RIP1 and RIP3 through RIP homotypic interaction motifs to activate NF-kappaB.

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Date

2009

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Périmètre
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Serveur académique Lausannois

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Ce document est lié à :
info:eu-repo/semantics/altIdentifier/doi/10.1038/embor.2009.109

Ce document est lié à :
info:eu-repo/semantics/altIdentifier/pmid/19590578

Ce document est lié à :
info:eu-repo/semantics/altIdentifier/urn/urn:nbn:ch:serval-BIB_98489985CB9E8

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Serveur Académique Lausannois

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Université de Lausanne et CHUV

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info:eu-repo/semantics/openAccess , Copying allowed only for non-profit organizations , https://serval.unil.ch/disclaimer

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Adaptor Proteins, Vesicular Transport/chemistry; Adaptor Proteins, Vesicular Transport/genetics; Animals; Binding Sites; Cell Line; DNA-Binding Proteins/genetics; DNA-Binding Proteins/metabolism; Glycoproteins/genetics; Glycoproteins/metabolism; Humans; Immunoblotting; Immunoprecipitation; Mice; NF-kappa B/metabolism; Nuclear Pore Complex Proteins/chemistry; Nuclear Pore Complex Proteins/genetics; Polymerase Chain Reaction; Protein Binding/genetics; Protein Binding/physiology; RNA-Binding Proteins/chemistry; RNA-Binding Proteins/genetics; Receptor-Interacting Protein Serine-Threonine Kinases/chemistry; Receptor-Interacting Protein Serine-Threonine Kinases/genetics

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Proteids Interferons

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M. Rebsamen et al., « DAI/ZBP1 recruits RIP1 and RIP3 through RIP homotypic interaction motifs to activate NF-kappaB. », Serveur académique Lausannois, ID : 10.1038/embor.2009.109

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Detection of viral nucleic acids is central to antiviral immunity. Recently, DAI/ZBP1 (DNA-dependent activator of IRFs/Z-DNA binding protein 1) was identified as a cytoplasmic DNA sensor and shown to activate the interferon regulatory factor (IRF) and nuclear factor-kappa B (NF-kappaB) transcription factors, leading to type-I interferon production. DAI-induced IRF activation depends on TANK-binding kinase 1 (TBK1), whereas signalling pathways and molecular components involved in NF-kappaB activation remain elusive. Here, we report the identification of two receptor-interacting protein (RIP) homotypic interaction motifs (RHIMs) in the DAI protein sequence, and show that these domains relay DAI-induced NF-kappaB signals through the recruitment of the RHIM-containing kinases RIP1 and RIP3. We show that knockdown of not only RIP1, but also RIP3 affects DAI-induced NF-kappaB activation. Importantly, RIP recruitment to DAI is inhibited by the RHIM-containing murine cytomegalovirus (MCMV) protein M45. These findings delineate the DAI signalling pathway to NF-kappaB and suggest a possible new immune modulation strategy of the MCMV.

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