The MAP kinase ERK5 binds to and phosphorylates p90 RSK
The MAP kinase ERK5 binds to and phosphorylates p90 RSK
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DOI：
10.1016/j.abb.2006.02.023
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发表时间：
2006-05-15
影响因子：
3.9
通讯作者：
Cobb, Melanie H.
中科院分区：
文献类型：
--
作者：
Ranganathan, Aarati;Pearson, Gray W.;Cobb, Melanie H.
我们先前表明，p90 RSK在表达活化的MEK 5突变体（MAP激酶ERK 5的激活剂）的细胞中被激活。基于以下证据，我们认为ERK 5可以直接激活细胞中的RSK。ERK 5在体外与RSK结合，并从细胞提取物中共免疫沉淀; ERK 5的活化减弱了其与RSK的结合，表明RSK在活化后释放。ERK 5在体外对RSK的磷酸化导致其活化，表明RSK是ERK 5的底物。在细胞中，ERK 5而不是p38或c-Jun N-末端激酶的活化与RSK活化相关。ERK 5的大C-末端结构域对于ERK 5结合或激活RSK不是必需的;然而，ERK 5的共同对接或CD结构域和RSK的对接或D结构域对于它们的关联是重要的。(c)2006爱思唯尔公司All rights reserved.
We showed previously that p90 RSK was activated in cells expressing an activated mutant of MEK5, the activator of the MAP kinase ERK5. Based on the following evidence, we suggest that ERK5 can directly activate RSK in cells. ERK5 binds to RSK in vitro and coimmunoprecipitates from cell extracts; activation of ERK5 weakens its binding to RSK, suggesting that RSK is released upon activation. Phosphorylation of RSK by ERK5 in vitro causes its activation, indicating that RSK is a substrate of ERK5. In cells activation of ERK5 but not p38 or the c-Jun N-terminal kinase is associated with RSK activation. The large C-terminal domain of ERK5 is not required for binding or activation of RSK by ERK5; however, the common docking or CD domain of ERK5 and the docking or D domain of RSK are important for their association. (c) 2006 Elsevier Inc. All rights reserved.