Identifi cation and functional analysis of phosphorylation residues of the Arabidopsis BOTRYTIS-INDUCED KINASE1

作     者：Jinhua Xu Xiaochao Wei Limin Yan Dan Liu Yuanyuan Ma Yu Guo Chune Peng Honggang Zhou Cheng Yang Zhiyong Lou Wenqing Shui 

作者机构：College of Life Sciences and Tianjin State Laboratory of Protein ScienceNankai UniversityTianjin 300071China High-throughput Molecular Drug Discovery CenterTianjin Joint Academy of Biotechnology and MedicineTianjin 300457China Laboratory of Structural Biology and MOE Laboratory of Protein ScienceSchool of Medicine and Life SciencesTsinghua UniversityBeijing 100084China College of Pharmacy and State Key Laboratory of Medicinal Chemical BiologyNankai UniversityTianjin 300071China 

出 版 物：《Protein & Cell》 (蛋白质与细胞（英文版）)

年 卷 期：2013年第4卷第10期

页      面：771-781页

核心收录：

学科分类：0710[理学-生物学] 071001[理学-植物学] 07[理学] 

基　　金：the National Natural Science Foundation of China(Grant Nos.31170782 and 31100208) Tianjin Natural Science Foundation(Grant No.11JCYBJC25500) Spe-cialized Research Fund for the Doctoral Program of Higher Education(Grant No.20110031120019) 

主　　题：phosphorylation BIK1 receptor-like cytop-lasmic kinase quantitative mass spectrometry 

摘      要：Arabidopsis BOTRYTIS-INDUCED KINASE1(BIK1)is a receptor-like cytoplasmic kinase acting early in multiple signaling pathways important for plant growth and innate *** is known to form a signaling complex with a cell-surface receptor FLS2 and a co-receptor kinase BAK1 to transduce signals upon perception of pathogen-asso-ciated molecular patterns(PAMPs).Although site-specifi c phosphorylation is speculated to mediate the activation and function of BIK1,few studies have been devoted to complete profiling of BIK1 phosphorylation ***,we identified nineteen in vitro autophosphoryla-tion sites of BIK1 including three phosphotyrosine sites,thereby proving BIK1 is a dual-specifi city kinase for the fi rst *** kinase activity of BIK1 substitution mutants were explicitly assessed using quantitative mass spec-trometry(MS).Thr-237,Thr-242 and Tyr-250 were found to most signifi cantly affect BIK1 activity in autophosphoryla-tion and phosphorylation of BAK1 in vitro.A structural model of BIK1 was built to further illustrate the molecular functions of specifi c phosphorylation *** also mapped new sites of FLS2 phosphorylation by BIK1,which are different from those by *** in vitro results could provide new hypotheses for more in-depth in vivo studies leading to deeper understanding of how phosphorylation contributes to BIK1 activation and medi-ates downstream signaling specifi city.