ArticleProtein & cell2013
Identification and functional analysis of phosphorylation residues of the Arabidopsis BOTRYTIS-INDUCED KINASE1.
Article in Protein & cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- The Ralstonia solanacearum E3 Ligase Effector RipV1 Targets Plant U-Box Domain-Containing Receptor-Like Cytoplasmic Kinases That Negatively Regulate Immunity in Nicotiana benthamiana.Molecular plant pathology · 2026Article
- Flagellin sensing, signaling, and immune responses in plants.Plant communications · 2025Review
- Mitogen-activated protein kinases MPK3 and MPK6 phosphorylate receptor-like cytoplasmic kinase CDL1 to regulate soybean basal immunity.The Plant cell · 2024Article
- Genomic Analysis Highlights Putative Defective Susceptibility Genes in Tomato Germplasm.Plants (Basel, Switzerland) · 2023Article
- Activation loop phosphorylation of a non-RD receptor kinase initiates plant innate immune signaling.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Importance of tyrosine phosphorylation for transmembrane signaling in plants.The Biochemical journal · 2021Review
- Phosphorylation-dependent subfunctionalization of the calcium-dependent protein kinase CPK28.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The MAP4 Kinase SIK1 Ensures Robust Extracellular ROS Burst and Antibacterial Immunity in Plants.Cell host & microbe · 2018Article
- Analysis of Phosphorylation of the Receptor-Like Protein Kinase HAESA during Arabidopsis Floral Abscission.PloS one · 2016Article
- New HDAC6-mediated deacetylation sites of tubulin in the mouse brain identified by quantitative mass spectrometry.Scientific reports · 2015Article
- Phosphorylation of trihelix transcriptional repressor ASR3 by MAP KINASE4 negatively regulates Arabidopsis immunity.The Plant cell · 2015Article
- The calcium-dependent protein kinase CPK28 negatively regulates the BIK1-mediated PAMP-induced calcium burst.Plant signaling & behavior · 2015Article
- Protein poly(ADP-ribosyl)ation regulates arabidopsis immune gene expression and defense responses.PLoS genetics · 2015Article
- Microbe-associated molecular pattern-induced calcium signaling requires the receptor-like cytoplasmic kinases, PBL1 and BIK1.BMC plant biology · 2014Article
- The growth-defense pivot: crisis management in plants mediated by LRR-RK surface receptors.Trends in biochemical sciences · 2014Review
- Negative control of BAK1 by protein phosphatase 2A during plant innate immunity.The EMBO journal · 2014Article
Corrections and comments
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
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-specific 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-specificity kinase for the first 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 significantly 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 specific 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 specificity.
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