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MSK1和MSK2介导有丝分裂原和应激诱导的组蛋白H3磷酸化:一个争议得以解决。

MSK1 and MSK2 mediate mitogen- and stress-induced phosphorylation of histone H3: a controversy resolved.

作者信息

Davie James R

机构信息

Manitoba Institute of Cell Biology, University of Manitoba, 675 McDermot Avenue, Winnipeg, Manitoba, Canada, R3E 0V9.

出版信息

Sci STKE. 2003 Aug 12;2003(195):PE33. doi: 10.1126/stke.2003.195.pe33.

Abstract

It is well established that mitogen- and stress-activated signal transduction pathways result in the rapid phosphorylation (Ser10 and Ser28) and acetylation of mammalian histone H3 associated with immediate-early genes. However, the prerequisite of H3 phosphorylation for the acetylation event and the identity of the mitogen-activated H3 kinase as RSK2 or MSK1 were controversial. A recent study with mouse embryonic fibroblasts lacking MSK1 and/or MSK2 demonstrated that MSK2 and MSK1 were the stimulus-induced H3 kinases and that neither of these enzyme activities was required for acetylation of H3 bound to immediate-early genes to occur.

摘要

众所周知,丝裂原和应激激活的信号转导途径会导致与即早基因相关的哺乳动物组蛋白H3快速磷酸化(Ser10和Ser28)和乙酰化。然而,H3磷酸化对于乙酰化事件的先决条件以及丝裂原激活的H3激酶是RSK2还是MSK1存在争议。最近一项针对缺乏MSK1和/或MSK2的小鼠胚胎成纤维细胞的研究表明,MSK2和MSK1是刺激诱导的H3激酶,并且这些酶活性都不是与即早基因结合的H3乙酰化发生所必需的。

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