蛋白磷酸化和泛素化等蛋白修饰是调节蛋白活性的重要方式。拟南芥类受体蛋白激酶FERONIA(FER)在植物生长发育及抗逆中起重要的作用。我们的前期研究显示，FER受体激酶信号通过激活ABI2磷酸酶，来抑制ABA信号(Yu et al,2012）。然而，FER活性如何被调控尚不清楚。而且，FER发育和抗逆的信号通路尚需进一步完善。通过酵母双杂，筛到2个E3连接酶(FEP1、FEP2)与FER互作，暗示FEP1和FEP2可能使FER泛素化，最终导致FER被降解从而抑制FER信号；或者FER使FEP1，FEP2磷酸化而改变它们的活性。在前期工作基础上，本项目拟分析fep突变体在抗真菌、营养生长、及激素响应中的表型；鉴定与FEP1，FEP2协作的E2结合酶；研究FEP1，FEP1泛素连接酶活性及FER磷酸化FEP1，FEP活性，为阐明FER信号通路奠定基础。

Protein modifications, such as protein phosphorylation and ubiquitination are pivotal ways to regulate protein activity. Arabidopsis receptor-like kinase FERONIA plays important roles in growth development and stress resistance.Our previous data showed that FER signal can suppress ABA signal by activating ABI2(Yu et al,2012). However,how FER activity be regulated remains unknown. Furthermore,there is a lot to learn in details about the signal transduction elements in the FER signal pathways.Two E3 ubiquitin-protein ligases,named as FEP1 and FEP2,were identified interacting with FER, suggesting FER might be ubiquitinated by E3 ligase FEP1 and FEP2, or FEP1 and FEP2 might be phosphorylated by kinase FER.Bassed on these findings, we will analyze the phenoype of fep1,fep2, fep1 fep2 mutants in pathogen-resistance, vegetative growth, and phytohormone responses, identify E2 conjugate(s) that cooperated with FEP1 and FEP2, dissect ubiquitinating activity on the combination of FEP1, FEP2 and the cooperated E2(s), and dissect the phosphorylating activity of FER as well.