ArticleThe Plant cell2020
Constitutive Activation of Leucine-Rich Repeat Receptor Kinase Signaling Pathways by BAK1-INTERACTING RECEPTOR-LIKE KINASE3 Chimera.
Article in The Plant cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 43 citations in OpenAlex.
- A disulfide bond sculpts the CTNIP4 phytocytokine fold for recognition by the receptor kinase HSL3.Nature plants · 2026Article
- A mechanistic framework for the recognition of chemically diverse brassinosteroids by BRI1-family receptor kinases.Nature plants · 2026Article
- The C-terminal tail of Cf resistance proteins determines the intensity of the effector-triggered hypersensitive response-related cell death.Plant physiology · 2026Article
- Regulation of stomatal development by receptor-like kinases and receptor-like proteins inFrontiers in plant science · 2026Review
- An AINTEGUMENTA phosphoswitch controls bilateral stem cell activity during secondary growth.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Genomic insights into the domestication and genetic basis of yield in papaya.Horticulture research · 2025Article
- Chemical genetics reveals cross-regulation of plant developmental signaling by the immune peptide-receptor pathway.Science advances · 2025Article
- Mechanistic Insights into the Function of 14-3-3 Proteins as Negative Regulators of Brassinosteroid Signaling in Arabidopsis.Plant & cell physiology · 2024Article
- The brassinosteroid receptor geneScience advances · 2024Article
- Chemical genetics reveals cross-activation of plant developmental signaling by the immune peptide-receptor pathway.bioRxiv : the preprint server for biology · 2024Article
- Small Peptides: Orchestrators of Plant Growth and Developmental Processes.International journal of molecular sciences · 2024Review
- Receptor-like cytoplasmic kinases of different subfamilies differentially regulate SOBIR1/BAK1-mediated immune responses in Nicotiana benthamiana.Nature communications · 2024Article
- New insights into QTNs and potential candidate genes governing rice yield via a multi-model genome-wide association study.BMC plant biology · 2024Article
- PSY-PSYR peptide-receptor pairs control the trade-off between plant growth and stress response.Plant signaling & behavior · 2023Article
- Asymmetric Evolution of Protein Domains in the Leucine-Rich Repeat Receptor-Like Kinase Family of Plant Signaling Proteins.Molecular biology and evolution · 2023Article
- Advances in Receptor-like Protein Kinases in Balancing Plant Growth and Stress Responses.Plants (Basel, Switzerland) · 2023Review
- Perception of a conserved family of plant signalling peptides by the receptor kinase HSL3.eLife · 2022Article
- HSL1 and BAM1/2 impact epidermal cell development by sensing distinct signaling peptides.Nature communications · 2022Article
- Engineering Chimeras by Fusing Plant Receptor-like Kinase EMS1 and BRI1 Reveals the Two Receptors' Structural Specificity and Molecular Mechanisms.International journal of molecular sciences · 2022Article
- 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
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
Receptor kinases with extracellular leucine-rich repeat domains (LRR-RKs) form the largest group of membrane signaling proteins in plants. LRR-RKs can sense small molecule, peptide, or protein ligands and may be activated by ligand-induced interaction with a shape complementary SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE (SERK) coreceptor kinase. We have previously shown that SERKs can also form constitutive, ligand-independent complexes with the LRR ectodomains of BAK1-INTERACTING RECEPTOR-LIKE KINASE3 (BIR3) receptor pseudokinases, negative regulators of LRR-RK signaling. Here, we report that receptor chimera in which the extracellular LRR domain of BIR3 is fused to the cytoplasmic kinase domains of the SERK-dependent LRR-RKs BRASSINOSTEROID INSENSITIVE1, HAESA and ERECTA form tight complexes with endogenous SERK coreceptors in the absence of ligand stimulus. Expression of these chimeras under the control of the endogenous promoter of the respective LRR-RK leads to strong gain-of-function brassinosteroid, floral abscission, and stomatal patterning phenotypes, respectively. Importantly, a BIR3-GASSHO1 (GSO1)/SCHENGEN3 (SGN3) chimera can partially complement
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