NIK and Cot cooperate to trigger NF-κB p65 phosphorylation

被引：14

作者：

Wittwer, Tobias ^{[1
]}

Schmitz, M. Lienhard ^{[1
]}

机构：

[1] Univ Giessen, Inst Biochem, Fac Med, D-35392 Giessen, Germany

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2008年 / 371卷 / 02期

关键词：

NF-kappa B; transactivation; phosphorylation; kinase; transcription;

D O I：

10.1016/j.bbrc.2008.04.069

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The serine/threonine kinase Cot triggers NF-kappa B-dependent transactivation and activation of various MAP-Kinases. 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-kappa B-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. Crown Copyright (C) 2008 Published by Elsevier Inc. All rights reserved.

引用

页码：294 / 297

页数：4

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