URGV Plant Genomics Laboratory, Evry, France.
Department of Plant Molecular Biology, Max F. Perutz Laboratories, University of Vienna, Vienna, Austria.
PeerJ. 2013 Apr 2;1:e59. doi: 10.7717/peerj.59. Print 2013.
So far little is known on the functional role of phosphorylation in the heat stress response of plants. Here we present evidence that heat stress activates the Arabidopsis mitogen-activated protein kinase MPK6. In vitro and in vivo evidence is provided that MPK6 specifically targets the major heat stress transcription factor HsfA2. Activation of MPK6 results in complex formation with HsfA2. MPK6 phosphorylates HsfA2 on T249 and changes its intracellular localisation. Protein kinase and phosphatase inhibitor studies indicate that HsfA2 protein stability is regulated in a phosphorylation-dependent manner, but this mechanism is independent of MPK6. Overall, our data show that heat stress-induced targeting of HsfA2 by MPK6 participates in the complex regulatory mechanism how plants respond to heat stress.
目前对于磷酸化在植物热应激反应中的功能作用知之甚少。在这里,我们提供的证据表明,热应激会激活拟南芥丝裂原活化蛋白激酶 MPK6。提供了体内和体外的证据表明,MPK6 特异性靶向主要的热应激转录因子 HsfA2。MPK6 的激活导致与 HsfA2 的复合物形成。MPK6 在 T249 上磷酸化 HsfA2 并改变其细胞内定位。蛋白激酶和磷酸酶抑制剂研究表明,HsfA2 蛋白稳定性的调节是一种依赖于磷酸化的方式,但这种机制与 MPK6 无关。总的来说,我们的数据表明,由 MPK6 诱导的 HsfA2 的热应激靶向参与了植物如何应对热应激的复杂调节机制。