J Integr Plant Biol. ›› 2018, Vol. 60 ›› Issue (2): 173-188.DOI: 10.1111/jipb.12614

• Research Articles • Previous Articles    

The calcium-dependent kinase OsCPK24 functions in cold stress responses in rice

Yu Liu1, Chunjue Xu2, Yanfen Zhu1, Lina Zhang1, Taiyu Chen1, Fei Zhou1, Hao Chen1 and Yongjun Lin1*   

  1. 1National Key Laboratory of Crop Genetic Improvement and National Center of Plant Gene Research (Wuhan), Huazhong Agricultural University, Wuhan 430070, China
    2Shenzhen Institute of Molecular Crop Design, Shenzhen 518107, China
  • Received:2017-08-02 Accepted:2017-11-23 Published:2018-02-13
  • About author:*Correspondence: Email: Yongjun Lin (yongjunlin@mail.hzau.edu.cn)


Calcium-dependent protein kinases (CPKs) are serine/threonine protein kinases that function in plant stress responses. Although CPKs are recognized as key messengers in signal transduction, the specific roles of CPKs and the molecular mechanisms underlying their activity remain largely unknown. Here, we characterized the function of OsCPK24, a cytosol-localized calcium-dependent protein kinase in rice. OsCPK24 was universally and highly expressed in rice plants and was induced by cold treatment. Whereas OsCPK24 knockdown plants exhibited increased sensitivity to cold compared to wild type (WT), OsCPK24-overexpressing plants exhibited increased cold tolerance. Plants overexpressing OsCPK24 exhibited increased accumulation of proline (an osmoprotectant) and glutathione (an antioxidant) and maintained a higher GSH/GSSG (reduced glutathione to oxidized glutathione) ratio during cold stress compared to WT. In addition to these effects in response to cold stress, we observed the kinase activity of OsCPK24 varied under different calcium concentrations. Further, OsCPK24 phosphorylated OsGrx10, a glutathione-dependent thioltransferase, at rates modulated by changes in calcium concentration. Together, our results support the hypothesis that OsCPK24 functions as a positive regulator of cold stress tolerance in rice, a process mediated by calcium signaling and involving phosphorylation and the inhibition of OsGrx10 to sustain higher glutathione levels.

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