植物利用免疫受体感知病原菌的入侵并激活防卫反应。前期我们研究发现，细胞质类受体激酶第七亚家族（RLCK VII）蛋白是连接位于细胞膜上的免疫受体与下游免疫信号的重要组分，在植物免疫信号传导途径中起关键作用，但是对该家族蛋白作用机制的研究还十分有限。本项目利用RLCK VII蛋白PBL19为靶蛋白，采用免疫共沉淀结合质谱技术鉴定了互作蛋白。拟通过荧光素酶互补实验及免疫共沉淀验证蛋白互作关系，并分析候选蛋白在植物免疫反应中的功能。基于前期对候选蛋白磷酸化位点的鉴定，通过分析磷酸化位点的调控方式及磷酸化修饰在植物免疫反应中的功能，解析RLCK VII蛋白与其互作蛋白调控植物免疫反应的分子机制。研究结果可进一步完善植物免疫反应的调控机制，为提高农作物的抗病性提供新的策略。

Plants employ immune receptors to perceive pathogens and trigger defense responses. Our previous work revealed that RLCK VII (Receptor-like cytoplasmic kinases VII) associated with cell surface located immune receptors are central for the activation of downstream signaling pathways. However, how RLCK VII activate downstream signaling components remains to be well studied. In this study, we identify PBL19-interacting proteins using co-immunoprecipitation followed by mass spectrometry. Next, we will confirm the interaction by luciferase complementation assay and co-immunoprecipitation, and analyze how the interacting protein function in plant immune responses. Base on the identification of phospho-sites in the interacting protein, we will analyze whether RLCK VII are responsible for the phosphorylation and the role of the phosphorylation in defense responses. The findings in this project will provide new insights into the molecular mechanisms of plant innate immunity, and provide novel resistance resource for plant breeding.