Motif-based substrate mapping of the receptor-like cytoplasmic kinase BIK1 reveals novel components and regulatory nodes of plant immunity

Plant cell surface pattern recognition receptors (PRRs) perceive non- or altered-self elicitors to induce immune responses. PRRs relay information across the plasma membrane and trigger downstream signalling via receptor-like cytoplasmic kinases such as BOTRYTIS-INDUCED KINASE 1 (BIK1). BIK1 associates with several PRRs and acts as a key executor of immune responses through the phosphorylation of substrate proteins. However, a comprehensive understanding of how BIK1 targets specific substrates and a full repertoire of these substrates are lacking. Here we defined the substrate specificity of BIK1 and used these data to predict candidate substrates in Arabidopsis. Using high-throughput biochemical and genetic screening of these candidates, we confirmed many as direct BIK1 substrates in vitro and novel regulators of plant immunity. Among the BIK1 substrates identified are MULTIPLE C2 DOMAIN AND TRANSMEMBRANE REGION PROTEIN 3, which we reveal regulates flagellin 22 (flg22)-induced plasmodesmata closure and immunity, and members of the largely uncharacterized CYCLIN-DEPENDENT KINASE-LIKE family, which we uncover as novel negative regulators of immunity. In parallel, we interrogated intracellular NUCLEOTIDE-BINDING LEUCINE-RICH REPEAT (NLR) immune receptors for potential BIK1 phosphorylation motifs and identified multiple NLRs as direct BIK1 substrates. We reveal that BIK1 phosphorylation regulates NLR oligomerization, thus controlling a key activation step for these immune receptors. Together, our unbiased biochemical screens shed light on the central role of BIK1 as a key kinase shaping multiple layers of plant immune signalling.

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Publication Details

Journal
Nature Plants
Published
2026-02-09
DOI
https://doi.org/10.1038/s41477-025-02218-z
Primary Topic
Plant-Microbe Interactions and Immunity
Type
article
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article

Motif-based substrate mapping of the receptor-like cytoplasmic kinase BIK1 reveals novel components and regulatory nodes of plant immunity

Emily M. Huntsman, Christine R. Faulkner, Sera Choi, Weibing Wang et al.
Nature Plants
Plant-Microbe Interactions and Immunity
article

Motif-based substrate mapping of the receptor-like cytoplasmic kinase BIK1 reveals novel components and regulatory nodes of plant immunity

Emily M. Huntsman, Christine R. Faulkner, Sera Choi, Weibing Wang, Emmanuelle Bayer, Beibei Song, Jared L. Johnson, Tomer M. Yaron, Julian Dindas, Laura Herold, Marta Bjornson, Kyle W. Bender, Jack Rhodes, Ryan Toth, Florian Schwanke, Atsuo T. Sasaki, Philipp Köster, Thomas A. DeFalco, Estee E. Tee, Jin Zhou, Heekyung Ahn, Anka Colo, Yoonyoung Lee, Frank L H Menke, Cyril Zipfel, Álvaro D. Fernández-Fernández, Jonathan D. G. Jones, Paul Derbyshire, Eleanor Khochaba, Marija Smokvarska, Marie Le Naour--Vernet
article en

Abstract

Plant cell surface pattern recognition receptors (PRRs) perceive non- or altered-self elicitors to induce immune responses. PRRs relay information across the plasma membrane and trigger downstream signalling via receptor-like cytoplasmic kinases such as BOTRYTIS-INDUCED KINASE 1 (BIK1). BIK1 associates with several PRRs and acts as a key executor of immune responses through the phosphorylation of substrate proteins. However, a comprehensive understanding of how BIK1 targets specific substrates and a full repertoire of these substrates are lacking. Here we defined the substrate specificity of BIK1 and used these data to predict candidate substrates in Arabidopsis. Using high-throughput biochemical and genetic screening of these candidates, we confirmed many as direct BIK1 substrates in vitro and novel regulators of plant immunity. Among the BIK1 substrates identified are MULTIPLE C2 DOMAIN AND TRANSMEMBRANE REGION PROTEIN 3, which we reveal regulates flagellin 22 (flg22)-induced plasmodesmata closure and immunity, and members of the largely uncharacterized CYCLIN-DEPENDENT KINASE-LIKE family, which we uncover as novel negative regulators of immunity. In parallel, we interrogated intracellular NUCLEOTIDE-BINDING LEUCINE-RICH REPEAT (NLR) immune receptors for potential BIK1 phosphorylation motifs and identified multiple NLRs as direct BIK1 substrates. We reveal that BIK1 phosphorylation regulates NLR oligomerization, thus controlling a key activation step for these immune receptors. Together, our unbiased biochemical screens shed light on the central role of BIK1 as a key kinase shaping multiple layers of plant immune signalling.

Nature PlantsVol. 12(2)
John Innes Centre (GB), University of East Anglia (GB), Western University (CA), Boston Children's Hospital (US), Centre National de la Recherche Scientifique (FR), The University of Sydney (AU), Harvard University (US), Université de Bordeaux (FR), Nanyang Technological University (SG), Chinese Academy of Sciences (CN), University of Zurich (CH), Cornell University (US), University of Münster (DE), Norwich Research Park (GB), Sainsbury Laboratory (GB), Dana-Farber Cancer Institute (US), Laboratoire de Biogenèse Membranaire (FR), Institute of Genetics and Developmental Biology (CN), Institute of Plant Biology (HU), Weill Cornell Medicine (US), University of California, Davis (US), University of Edinburgh (GB)
Openalex Percentile: Top 61%
Plant-Microbe Interactions and Immunity
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