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MAP 激酶底物的探索:渐入佳境。

The Quest for MAP Kinase Substrates: Gaining Momentum.

机构信息

Institute of Agriculture, Centre for Agricultural Research of the Hungarian Academy of Sciences, Brunszvik utca 2, H-2462 Martonvásár, Hungary.

School of Biological Sciences and Centre for Systems and Synthetic Biology, Royal Holloway, University of London, Egham TW20 0EX, UK.

出版信息

Trends Plant Sci. 2018 Oct;23(10):918-932. doi: 10.1016/j.tplants.2018.08.002. Epub 2018 Aug 22.

Abstract

Mitogen-activated protein kinase (MAPK) pathways are versatile signaling mechanisms in all eukaryotes. Their signaling outputs are defined by the protein substrates phosphorylated by MAPKs. An expanding list of substrates has been identified by high-throughput screens and targeted approaches in plants. The majority of these are phosphorylated by MPK3/6, and a few by MPK4, which are the best-characterized plant MAPKs, participating in the regulation of numerous biological processes. The identified substrates clearly represent the functional diversity of MAPKs: they are associated with pathogen defense, abiotic stress responses, ethylene signaling, and various developmental functions. Understanding their outputs is integral to unraveling the complex regulatory mechanisms of MAPK cascades. We review here methodological approaches and provide an overview of known MAPK substrates.

摘要

丝裂原活化蛋白激酶(MAPK)途径是所有真核生物中通用的信号转导机制。它们的信号输出由 MAPK 磷酸化的蛋白质底物决定。通过高通量筛选和植物的靶向方法,已经确定了越来越多的底物。这些底物中的大多数被 MPK3/6 磷酸化,少数被 MPK4 磷酸化,MPK4 是研究最充分的植物 MAPK,参与了许多生物过程的调节。已鉴定的底物清楚地代表了 MAPK 的功能多样性:它们与病原体防御、非生物胁迫反应、乙烯信号和各种发育功能有关。了解它们的输出对于揭示 MAPK 级联的复杂调控机制至关重要。在这里,我们综述了方法学方法,并概述了已知的 MAPK 底物。

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