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Assessment of BAK1 activity in different plant receptor-like kinase complexes by quantitative profiling of phosphorylation patterns

文献类型：期刊论文

作者Wang, Yilin1,2; Li, Zhucui1,2; Liu, Dan1,2; Xu, Jinhua1,2; Wei, Xiaochao1,2; Yan, Liming3,4; Yang, Cheng2,5; Lou, Zhiyong3,4; Shui, Wenqing1,6
刊名JOURNAL OF PROTEOMICS
出版日期2014-08-28
卷号108期号:108页码:484-493
关键词BAK1 Plant receptor-like kinase Phosphorylation pattern profiling Label-free mass spectrometry
英文摘要Plant receptor-like kinases (RLKs) constitute a large family of receptors coordinating developmental programs with adaptation to environmental stresses including immune defenses. BRI1-ASSOCIATED KINASE 1 (BAK1), a member of the plant RLK family, forms receptor complexes with multiple RLK proteins including BRI1, FLS2, EFR and BIK1 to regulate responses to growth hormones or PAMPs. RLK activation and signal initiation involve protein complex formation and phosphorylation/dephosphorylation between BAK1 and its interacting partners. To gain new insight into how phosphorylation contributes to BAK1-mediated signaling specificity, we first mapped the phosphorylation patterns of BAK1 associated with different RLK partners (BRI1, FLS2, EFR and BIK1). Quantitative phospho-pattern profiling by label-free mass spectrometry revealed that differential phosphorylation patterns of RLK partners resulted from altered BAK1 phosphorylation status. More interestingly, the study of two BAK1 mutants (T450A and C408Y) both showing severe defect in immune defense yet normal growth phenotype suggested that varied phosphorylation patterns of RLK partners by BAK1 could be the molecular basis for selective regulation of multiple BAK1-dependent pathways. Taken together, this phospho-pattern profiling strategy allowed for explicit assessment of BAK1 kinase activity in different ELK complexes, which would facilitate elucidation of BAK1 diverse functions in plant development, defense, and adaptation.
WOS标题词Science & Technology ; Life Sciences & Biomedicine
类目[WOS]Biochemical Research Methods
研究领域[WOS]Biochemistry & Molecular Biology
关键词[WOS]BRASSINOSTEROID SIGNAL-TRANSDUCTION ; BOTRYTIS-INDUCED KINASE1 ; FUNCTIONAL-ANALYSIS ; IN-VITRO ; ARABIDOPSIS ; IDENTIFICATION ; ACTIVATION ; BRI1/BAK1 ; FLAGELLIN ; RESIDUES
收录类别SCI
语种英语
WOS记录号WOS:000340315400036
公开日期2014-11-25
源URL[http://124.16.173.210/handle/311007/497]  
专题天津工业生物技术研究所_生物质谱与定量生物学研究 水雯箐_期刊论文
作者单位1.Nankai Univ, Tianjin Key Lab Prot Sci, Coll Life Sci, Tianjin 300071, Peoples R China
2.Tianjin Joint Acad Biotechnol & Med, High Throughput Mol Drug Discovery Ctr, Tianjin 300457, Peoples R China
3.Tsinghua Univ, Sch Med & Life Sci, Struct Biol Lab, Beijing 100084, Peoples R China
4.Tsinghua Univ, Sch Med & Life Sci, MOE Lab Prot Sci, Beijing 100084, Peoples R China
5.Nankai Univ, State Key Lab Med Chem Biol, Tianjin 300071, Peoples R China
6.Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Tianjin 300308, Peoples R China
推荐引用方式
GB/T 7714		 Wang, Yilin,Li, Zhucui,Liu, Dan,et al. Assessment of BAK1 activity in different plant receptor-like kinase complexes by quantitative profiling of phosphorylation patterns[J]. JOURNAL OF PROTEOMICS,2014,108(108):484-493.
APA Wang, Yilin.,Li, Zhucui.,Liu, Dan.,Xu, Jinhua.,Wei, Xiaochao.,...&Shui, Wenqing.(2014).Assessment of BAK1 activity in different plant receptor-like kinase complexes by quantitative profiling of phosphorylation patterns.JOURNAL OF PROTEOMICS,108(108),484-493.
MLA Wang, Yilin,et al."Assessment of BAK1 activity in different plant receptor-like kinase complexes by quantitative profiling of phosphorylation patterns".JOURNAL OF PROTEOMICS 108.108(2014):484-493.

入库方式： OAI收割

来源：天津工业生物技术研究所

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