Viral dsRNA:TLR3:TRIF complex recruits RIP1

Stable Identifier
R-HSA-168930
Type
Reaction [binding]
Species
Homo sapiens
Related Species
Influenza A virus, Rotavirus, Hepatitis B virus, Hepatitis C Virus, Human herpesvirus 1
Compartment
ReviewStatus
5/5
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RIP1 is recruited to the activated TLR receptor by binding to TICAM1(TRIF) via its RHIM motif, followed by its polyubiquitination. Polyubiquitination is possibly mediated by TRAF6 that is also recruited to TICAM1 (Cusson-Hermance N et al. 2005). Other E3-ubiquitin ligases - cIAP1 and cIAP2 - have been reported to promote polyubiquitination of RIP proteins (Bertrand MJM et al. 2011).

RIP3 was shown to inhibit TRIF-induced NFkB activation in dose-dependent manner when overexpressed in HEK293T cells by competing with TRIF to bind RIP1 (Meylan E et al. 2004).

Literature References
PubMed ID Title Journal Year
16115877 Rip1 mediates the Trif-dependent toll-like receptor 3- and 4-induced NF-{kappa}B activation but does not contribute to interferon regulatory factor 3 activation

Fitzgerald, KA, Cusson-Hermance, N, Khurana, S, Kelliher, MA, Lee, TH

J Biol Chem 2005
15064760 RIP1 is an essential mediator of Toll-like receptor 3-induced NF-kappa B

Blancheteau, V, Meylan, E, Burns, K, Kelliher, M, Tschopp, J, Martinon, F, Hofmann, K

Nat Immunol 2004
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