ArticleThe Plant journal : for cell and molecular biology2014
Crystal structures of the phosphorylated BRI1 kinase domain and implications for brassinosteroid signal initiation.
Article in The Plant journal : for cell and molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.
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83 citing papers in PubMed, 170 citations in OpenAlex.
- A mechanistic framework for the recognition of chemically diverse brassinosteroids by BRI1-family receptor kinases.Nature plants · 2026Article
- Structural basis of OsCERK1-mediated signal activation and transduction in rice immunity and symbiosis.Plant communications · 2026Article
- Artificial intelligence-based structural modeling of PSTOL1 receptor kinases in rice and sorghum.Frontiers in plant science · 2026Article
- Unveiling FERONIA receptor kinase-mediated cellular mechanisms with a small-molecule inhibitor.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Induced variation in BRASSINOSTEROID INSENSITIVE 1 (BRI1) confers a compact wheat architecture.BMC plant biology · 2025Article
- Genome-Wide Identification and Functional Prediction of LRR-RLK Family Genes in Foxtail Millet (International journal of molecular sciences · 2025Article
- Preventing inappropriate signals pre- and post-ligand perception by a toggle switch mechanism of ERECTA.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- "Cyclic nucleotides in plants: from obscure messengers to central regulators".Frontiers in plant science · 2025Review
- Mechanistic Insights into the Function of 14-3-3 Proteins as Negative Regulators of Brassinosteroid Signaling in Arabidopsis.Plant & cell physiology · 2024Article
- Genomic Survey of LRR-RLK Genes inPlants (Basel, Switzerland) · 2024Article
- Characterization, evolution, and abiotic stress responses of leucine-rich repeat receptor-like protein kinases (LRR-RLK) in Liriodendron chinense.BMC genomics · 2024Article
- Molecular Lesions in BRI1 and Its Orthologs in the Plant Kingdom.International journal of molecular sciences · 2024Review
- Structural and biochemical basis of FLS2-mediated signal activation and transduction in rice.Plant communications · 2024Article
- The cell surface is the place to be for brassinosteroid perception and responses.Nature plants · 2024Review
- An update on evolutionary, structural, and functional studies of receptor-like kinases in plants.Frontiers in plant science · 2024Review
- PhosBoost: Improved phosphorylation prediction recall using gradient boosting and protein language models.Plant direct · 2023Article
- Structural and biochemical basis of Arabidopsis FERONIA receptor kinase-mediated early signaling initiation.Plant communications · 2023Article
- A point mutation in the kinase domain of CRK10 leads to xylem vessel collapse and activation of defence responses in Arabidopsis.Journal of experimental botany · 2023Article
- Potato protein tyrosine phosphatase StPTP1a is activated by StMKK1 to negatively regulate plant immunity.Plant biotechnology journal · 2023Article
- Receptor-like cytoplasmic kinase ScRIPK in sugarcane regulates disease resistance and drought tolerance inFrontiers in plant science · 2023Article
23 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Brassinosteroids, which control plant growth and development, are sensed by the membrane receptor kinase BRASSINOSTEROID INSENSITIVE 1 (BRI1). Brassinosteroid binding to the BRI1 leucine-rich repeat (LRR) domain induces heteromerisation with a SOMATIC EMBRYOGENESIS RECEPTOR KINASE (SERK)-family co-receptor. This process allows the cytoplasmic kinase domains of BRI1 and SERK to interact, trans-phosphorylate and activate each other. Here we report crystal structures of the BRI1 kinase domain in its activated form and in complex with nucleotides. BRI1 has structural features reminiscent of both serine/threonine and tyrosine kinases, providing insight into the evolution of dual-specificity kinases in plants. Phosphorylation of Thr1039, Ser1042 and Ser1044 causes formation of a catalytically competent activation loop. Mapping previously identified serine/threonine and tyrosine phosphorylation sites onto the structure, we analyse their contribution to brassinosteroid signaling. The location of known genetic missense alleles provide detailed insight into the BRI1 kinase mechanism, while our analyses are inconsistent with a previously reported guanylate cyclase activity. We identify a protein interaction surface on the C-terminal lobe of the kinase and demonstrate that the isolated BRI1, SERK2 and SERK3 cytoplasmic segments form homodimers in solution and have a weak tendency to heteromerise. We propose a model in which heterodimerisation of the BRI1 and SERK ectodomains brings their cytoplasmic kinase domains in a catalytically competent arrangement, an interaction that can be modulated by the BRI1 inhibitor protein BKI1.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.