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MAPK 底物识别和调控的模式。

Modes of MAPK substrate recognition and control.

机构信息

Department of Applied Genetics and Cell Biology (DAGZ), University of Natural Resources and Applied Life Sciences (BOKU), Muthgasse 18, Vienna A-1190, Austria.

出版信息

Trends Plant Sci. 2015 Jan;20(1):49-55. doi: 10.1016/j.tplants.2014.09.006. Epub 2014 Oct 6.

Abstract

Mitogen-activated protein kinase (MAPK) cascades are universal, evolutionary conserved signalling modules, which translate environmental information into appropriate responses via phosphorylation of their substrate proteins. In Arabidopsis, the MAPK MPK3 regulates numerous cellular processes, including the adaptation to abiotic and biotic stresses. The molecular steps immediately downstream of MPK3 induction have, therefore, received abundant attention, and a respectable number of MPK3 targets are known by now. These proteins illustrate the substrate promiscuity of MPK3. They also are evidence for how manifold phosphorylation-regulated functions can be. This review presents the current knowledge about the function and regulation of MPK3-targeted proteins, takes a close look at their primary protein sequences, and proposes a model of how MPK3 recognises, binds, and phosphorylates its targets.

摘要

丝裂原活化蛋白激酶(MAPK)级联是普遍存在且进化上保守的信号模块,通过其底物蛋白的磷酸化将环境信息转化为适当的反应。在拟南芥中,MAPK MPK3 调节许多细胞过程,包括对非生物和生物胁迫的适应。因此,MPK3 诱导后的分子步骤受到了广泛关注,现在已经知道了相当数量的 MPK3 靶标。这些蛋白质说明了 MPK3 的底物混杂性。它们还证明了磷酸化调节功能可以有多种形式。这篇综述介绍了关于 MPK3 靶向蛋白的功能和调节的最新知识,仔细研究了它们的一级蛋白质序列,并提出了一个模型,说明 MPK3 如何识别、结合和磷酸化其靶标。

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