| Literature DB >> 23638397 |
Alexandre Evrard1, Mukesh Kumar2, David Lecourieux3, Jessica Lucks4, Pascal von Koskull-Döring5, Heribert Hirt1.
Abstract
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.Entities:
Keywords: Arabidopsis; Heat stress proteins; Heat stress transcription factors; Kinases; MAP kinase
Year: 2013 PMID: 23638397 PMCID: PMC3628891 DOI: 10.7717/peerj.59
Source DB: PubMed Journal: PeerJ ISSN: 2167-8359 Impact factor: 2.984