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

文献类型： 外文期刊

作者： Wang, Bin 1 ; Fang, Ruiqiu 1 ; Zhang, Jia 1 ; Han, Jingluan 1 ; Chen, Faming 1 ; He, Furong 1 ; Liu, Yao-Guang 1 ; Chen, 1 ;

作者机构： 1.South China Agr Univ, State Key Lab Conservat & Utilizat Subtrop Agrobi, Guangzhou 510642, Peoples R China

2.South China Agr Univ, Guangdong Prov Key Lab Prot Funct & Regulat Agr O, Guangzhou 510642, Peoples R China

3.Guangdong Lab Lingnan Modern Agr, Guangzhou 510642, Peoples R China

4.South China Agr Univ, Coll Life Sci, Guangzhou 510642, Peoples R China

5.Zhejiang Acad Agr Sci, Dongyang Inst Maize Res, Dongyang 322100, Zhejiang, Peoples R China

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.

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