Rice LecRK5 phosphorylates a UGPase to regulate callose biosynthesis during pollen development

文献类型： 外文期刊

第一作者： Wang, Bin

作者： Wang, Bin;Fang, Ruiqiu;Zhang, Jia;Han, Jingluan;Chen, Faming;He, Furong;Liu, Yao-Guang;Chen, Letian;Wang, Bin;Han, Jingluan;Chen, Letian;Wang, Bin;Han, Jingluan;Liu, Yao-Guang;Chen, Letian;Wang, Bin;Zhang, Jia;Han, Jingluan;Chen, Faming;He, Furong;Liu, Yao-Guang;Chen, Letian;Fang, Ruiqiu

作者机构：

关键词： Callose; lectin receptor-like kinase; Oryza sativa; pollen development; rice; UGPase

期刊名称：JOURNAL OF EXPERIMENTAL BOTANY （ 影响因子：6.992； 五年影响因子：7.86 ）

ISSN： 0022-0957

年卷期： 2020 年 71 卷 14 期

页码：

收录情况： SCI

摘要： The temporary callose layer surrounding the tetrads of microspores is critical for male gametophyte development in flowering plants, as abnormal callose deposition can lead to microspore abortion. A sophisticated signaling network regulates callose biosynthesis but these pathways are poorly understood. In this study, we characterized a rice male-sterile mutant, oslecrk5, which showed defective callose deposition during meiosis. OsLecRK5 encodes a plasma membrane-localized lectin receptor-like kinase, which can form a dimer with itself. Moreover, normal anther development requires the K-phosphorylation site (a conserved residue at the ATP-binding site) of OsLecRK5. In vitro assay showed that OsLecRK5 phosphorylates the callose synthesis enzyme UGP1, enhancing callose biosynthesis during anther development. Together, our results demonstrate that plasma membrane-localized OsLecRK5 phosphorylates UGP1 and promotes its activity in callose biosynthesis in rice. This is the first evidence that a receptor-like kinase positively regulates callose biosynthesis.

分类号：

  • 相关文献
作者其他论文 更多>>

微信小程序