RIP proteins are receptor-interacting serine/threonine-protein kinases or cell death proteins [1]. This interacting domain is involved in virus recognition. The RHIM domain is necessary for the recruitment of RIP and RIP3 by the IFN-inducible protein DNA-dependent activator of IRFs (DAI), also known as DLM-1 or Z-DNA binding protein (ZBP1). Both the RIP kinases contribute to DAI-induced NF-kappaB activation. RIP3 undergoes auto phosphorylation on binding to DAI [2]. [1]. 11734559. Identification of a novel homotypic interaction motif required. for the phosphorylation of receptor-interacting protein (RIP) by. RIP3.. Sun X, Yin J, Starovasnik MA, Fairbrother WJ, Dixit VM;. J Biol Chem. 2002;277:9505-9511.. [2]. 19590578. DAI/ZBP1 recruits RIP1 and RIP3 through RIP homotypic. interaction motifs to activate NF-kappaB.. Rebsamen M, Heinz LX, Meylan E, Michallet MC, Schroder K,. Hofmann K, Vazquez J, Benedict CA, Tschopp J;. EMBO Rep. 2009;10:916-922. (from Pfam)
- Date:
- 2024-08-14