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Protein & Cell

ISSN 1674-800X

ISSN 1674-8018(Online)

CN 11-5886/Q

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Prot Cell    2013, Vol. 4 Issue (10) : 771-781    https://doi.org/10.1007/s13238-013-3053-6      PMID: 24104392
RESEARCH ARTICLE
Identification and functional analysis of phosphorylation residues of the Arabidopsis BOTRYTIS-INDUCED KINASE1
Jinhua Xu1,2, Xiaochao Wei1,2, Limin Yan3, Dan Liu1,2, Yuanyuan Ma3, Yu Guo2,4, Chune Peng1,2, Honggang Zhou2,4, Cheng Yang2,4, Zhiyong Lou3(), W enqing Shui1,2()
1. College of Life Sciences and Tianjin State Laboratory of Protein Science, Nankai University, Tianjin 300071, China; 2. High-throughput Molecular Drug Discovery Center, Tianjin Joint Academy of Biotechnology and Medicine, Tianjin 300457, China; 3. Laboratory of Structural Biology and MOE Laboratory of Protein Science, School of Medicine and Life Sciences, Tsinghua University, Beijing 100084, China; 4. College of Pharmacy and State Key Laboratory of Medicinal Chemical Biology, Nankai University, Tianjin 300071, China
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Abstract

Arabidopsis BOTRYTIS-INDUCED KINASE1 (BIK1) is a receptor-like cytoplasmic kinase acting early in multiple signaling pathways important for plant growth and innate immunity. It 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-associated 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 residues. Here, we identified nineteen in vitro autophosphorylation sites of BIK1 including three phosphotyrosine sites, thereby proving BIK1 is a dual-specifi city kinase for the fi rst time. The kinase activity of BIK1 substitution mutants were explicitly assessed using quantitative mass spectrometry (MS). Thr-237, Thr-242 and Tyr-250 were found to most signifi cantly affect BIK1 activity in autophosphorylation and phosphorylation of BAK1 in vitro. A structural model of BIK1 was built to further illustrate the molecular functions of specifi c phosphorylation residues. We also mapped new sites of FLS2 phosphorylation by BIK1, which are different from those by BAK1. These 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 mediates downstream signaling specifi city.
Keywords phosphorylation      BIK1      receptor-like cytoplasmic kinase      quantitative mass spectrometry     
Corresponding Author(s): Lou Zhiyong,Email:louzy@xtal.tsinghua.edu.cn; Shui W enqing,Email:angelshui@nankai.edu.cn   
Issue Date: 01 October 2013
 Cite this article:   
Jinhua Xu,Xiaochao Wei,Limin Yan, et al. Identification and functional analysis of phosphorylation residues of the Arabidopsis BOTRYTIS-INDUCED KINASE1[J]. Prot Cell, 2013, 4(10): 771-781.
 URL:  
https://academic.hep.com.cn/pac/EN/10.1007/s13238-013-3053-6
https://academic.hep.com.cn/pac/EN/Y2013/V4/I10/771
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