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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Structural basis for the recruitment of the human CCR4-NOT deadenylase complex by tristetraprolin.

Tristetraprolin (TTP) is an RNA-binding protein that controls the inflammatory response by limiting the expression of several proinflammatory cytokines. TTP post-transcriptionally represses gene expression by interacting with AU-rich elements (AREs) in 3' untranslated regions of target mRNAs and subsequently engenders their deadenylation and decay. TTP accomplishes these tasks, at least in part, by recruiting the multisubunit CCR4-NOT deadenylase complex to the mRNA. Here we identify an evolutionarily conserved C-terminal motif in human TTP that directly binds a central domain of CNOT1, a core subunit of the CCR4-NOT complex. A high-resolution crystal structure of the TTP-CNOT1 complex was determined, providing the first structural insight, to our knowledge, into an ARE-binding protein bound to the CCR4-NOT complex. Mutations at the CNOT1-TTP interface impair TTP-mediated deadenylation, demonstrating the significance of this interaction in TTP-mediated gene silencing.[1]


  1. Structural basis for the recruitment of the human CCR4-NOT deadenylase complex by tristetraprolin. Fabian, M.R., Frank, F., Rouya, C., Siddiqui, N., Lai, W.S., Karetnikov, A., Blackshear, P.J., Nagar, B., Sonenberg, N. Nat. Struct. Mol. Biol. (2013) [Pubmed]
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