The Blue Light-Dependent Phosphorylation of the CCE Domain Determines the Photosensitivity of Arabidopsis CRY2

文献类型： 外文期刊

第一作者： Wang, Qin

作者： Wang, Qin;Wang, Qin;He, Reqing;Liu, Xuanming;Zhao, Xiaoying;Barshop, William D.;Vashisht, Ajay A.;Wohlschlegel, James A.;Bian, Mingdi;Liu, Bin;Wang, Qin;Yu, Xuhong;Nguyen, Paula;Lin, Chentao

作者机构：

关键词： light regulation;light signaling;physiology of plant growth;Arabidopsis

期刊名称：MOLECULAR PLANT （ 影响因子：13.164； 五年影响因子：16.357 ）

ISSN： 1674-2052

年卷期： 2015 年 8 卷 4 期

页码：

收录情况： SCI

摘要： Arabidopsis cryptochrome 2 (CRY2) is a blue light receptor that mediates light inhibition of hypocotyl elongation and long-day promotion of floral initiation. CRY2 is known to undergo blue light-dependent phosphorylation, which is believed to serve regulatory roles in the function of CRY2. We report here on a biochemical and genetics study of CRY2 phosphorylation. Using mass spectrometry analysis, we identified three serine residues in the CCE domain of CRY2 (S588, S599, and S605) that undergo blue light-dependent phosphorylation in Arabidopsis seedlings. A study of serine-substitution mutations in the CCE domain of CRY2 demonstrates that CRY2 contains two types of phosphorylation in the CCE domain, one in the serine cluster that causes electrophoretic mobility upshift and the other outside the serine cluster that does not seem to cause mobility upshift. We showed that mutations in the serine residues within and outside the serine cluster diminished blue light-dependent CRY2 phosphorylation, degradation, and physiological activities. These results support the hypothesis that blue light-dependent phosphorylation of the CCE domain determines the photosensitivity of Arabidopsis CRY2.

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