Structural basis for the impact of phosphorylation on the activation of plant receptor-like kinase BAK1

Yan, Liming; Ma, Yuanyuan; Liú, Dan; Wei, Xiaochao; Sun, Yuna; Chen, Xiaoyue; Zhao, Huadong; Zhou, Jingwen; Wang, Wenfei; Wang, Shui; Lou, Zhiyong

doi:10.1038/cr.2012.74

Cited by 81 publications

(127 citation statements)

References 15 publications

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“…Whether they modify the same residues of FLS2 is unknown. Herein we identified the residues in FLS2-CD phosphorylated by BIK1 and compared with those by BAK1 reported by our previous study (Yan et al, 2012). It turned out that the two kinases showed differential selectivity in substrate sequences, as summarized in Fig.…”

Section: Bik1 and Bak1 Phosphorylate A Bacterial Pamp-receptor Fls2 Amentioning

confidence: 99%

“…Using a sensitive workflow combining phosphopeptide enrichment and nan oLC-MS/MS analysis (Yan et al, 2012), we were able to unambiguously map 16 Ser/Thr autophosphorylation sites on BIK1 (Fig. 1B, see details of MS analysis in Table S3 and Fig.…”

Section: Identifi Cation Of Bik1 Autophosphorylation Residues and Resmentioning

confidence: 99%

“…The cytoplasmic kinase domains of the two RLKs were reported to phosphorylate FLS2 in vitro (Lu et al, 2010a;Yan et al, 2012) (Fig. 1A).…”

Section: Bik1 and Bak1 Phosphorylate A Bacterial Pamp-receptor Fls2 Amentioning

confidence: 99%

“…Two residues (Ser-906 and Ser-1115) in the kinase domain of FLS2 were phosphorylated by both kinases, and other residues were distinctly targeted by a specifi c kinase. All of these (Yan et al, 2012), including the four Ser/Thr residues in its AL also phosphorylated in vivo upon brassinolide treatment (Wang et al, 2008). Notably, Thr-455 in BAK1 AL phosphorylated by BIK1 was shown to be critical for BAK1 kinase activity as well as its function in BR and fl agellin signaling (Wang et al, 2008).…”

Section: Bik1 and Bak1 Phosphorylate A Bacterial Pamp-receptor Fls2 Amentioning

confidence: 99%

“…In addition, reciprocal phosphorylation occurs between BIK1 and BAK1. In contrast to BAK1 on which distinctive phosphorylation sites have been clearly identifi ed (Wang et al, 2005(Wang et al, , 2008Yan et al, 2012), few studies have been devoted to complete profi ling of phosphorylation residues of BIK1. Biochemical analysis of site-directed mutants suggested Thr-237 was the major phosphorylation site of BIK1 in response to fl agellin (Lu et al, 2010a).…”

Section: Introductionmentioning

confidence: 99%

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

Wei

Lin

et al. 2013

Protein Cell

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Arabidopsis BOTRYTIS-INDUCED KINASE1 (BIK1) is areceptor-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.

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Section: Bik1 and Bak1 Phosphorylate A Bacterial Pamp-receptor Fls2 Amentioning

confidence: 99%

Section: Identifi Cation Of Bik1 Autophosphorylation Residues and Resmentioning

confidence: 99%

“…The cytoplasmic kinase domains of the two RLKs were reported to phosphorylate FLS2 in vitro (Lu et al, 2010a;Yan et al, 2012) (Fig. 1A).…”

Section: Bik1 and Bak1 Phosphorylate A Bacterial Pamp-receptor Fls2 Amentioning

confidence: 99%

Section: Bik1 and Bak1 Phosphorylate A Bacterial Pamp-receptor Fls2 Amentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

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

Wei

Lin

et al. 2013

Protein Cell

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Brassinosteroid Sensing and Signaling in Plants

Hohmann

Hothorn

2018

Plant Structural Biology: Hormonal Regulations

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Inceptin: Exploring Its Role as a Peptide Elicitor in Plant Defense Mechanisms

Sharma,

Singh

2024

Plant Elicitor Peptides

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Structural basis for the impact of phosphorylation on the activation of plant receptor-like kinase BAK1

Cited by 81 publications

References 15 publications

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

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

Brassinosteroid Sensing and Signaling in Plants

Inceptin: Exploring Its Role as a Peptide Elicitor in Plant Defense Mechanisms

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