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Publication : NIK and Cot cooperate to trigger NF-kappaB p65 phosphorylation.

First Author  Wittwer T Year  2008
Journal  Biochem Biophys Res Commun Volume  371
Issue  2 Pages  294-7
PubMed ID  18439422 Mgi Jnum  J:136251
Mgi Id  MGI:3795794 Doi  10.1016/j.bbrc.2008.04.069
Citation  Wittwer T, et al. (2008) NIK and Cot cooperate to trigger NF-kappaB p65 phosphorylation. Biochem Biophys Res Commun 371(2):294-7
abstractText  The serine/threonine kinase Cot triggers NF-kappaB-dependent transactivation and activation of various MAPKinases. Here we identify Cot as a novel p65 interacting protein kinase. Cot expression induces p65 phosphorylation at serines 536 and 468 in dependence from its kinase function. Accordingly, shRNA-mediated knockdown of Cot expression interferes with TNF-induced NF-kappaB-dependent gene expression. Also the C-terminally truncated, oncogenic form of Cot is able to trigger p65 phosphorylation. In vitro kinase assays and dominant negative mutants revealed that NIK functions downstream of Cot to mediate p65 phosphorylation.
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