ArticlePlant physiology2016
OsBRI1 Activates BR Signaling by Preventing Binding between the TPR and Kinase Domains of OsBSK3 via Phosphorylation.
Article in Plant physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
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Who cites it
61 citing papers in PubMed.
- Deletion of TaBSK3-2B attenuates BR signaling to regulate the Rht4 semi-dwarf phenotype and drought tolerance in wheat.The Plant journal : for cell and molecular biology · 2026Article
- The GSK3/SHAGGY-like OsGSK3 phosphorylates and inhibits phase separation of OsFCA at Ser-43 and Ser-45 to regulate brassinosteroid signaling and rice architecture.The New phytologist · 2026Article
- SSR marker development for analysis of the genetic diversity and identification of species and infraspecific ranks in the genus Phyllostachys.BMC plant biology · 2026Article
- Harnessing brassinosteroid signaling in rice: from molecular pathways to environmentally adaptive breeding.Frontiers in plant science · 2026Review
- Rice ETHYLENE RESPONSE FACTOR 101 increases leaf angle by upregulating BRASSINOSTEROID UPREGULATED 1.The Plant journal : for cell and molecular biology · 2025Article
- OsMAPKKK5 affects brassinosteroid signal transduction via phosphorylating OsBSK1-1 and regulates rice plant architecture and yield.Plant biotechnology journal · 2025Article
- Rice grain size: current regulatory mechanisms and future perspectives.Journal of plant research · 2025Review
- OsBSK3 and OsBSK2 regulate grain size and leaf angle via MAPK signaling pathway in rice.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2025Article
- Prioritization of candidate genes regulating the dwarfness in rice by integration of whole-genome and transcriptome analyses.Functional & integrative genomics · 2025Article
- The rice R2R3 MYB transcription factor FOUR LIPS connects brassinosteroid signaling to lignin deposition and leaf angle.The Plant cell · 2024Article
- Genome-Wide Identification of the Brassinosteroid Signal Kinase Gene Family and Its Profiling under Salinity Stress.International journal of molecular sciences · 2024Article
- The protein phosphatase qGL3/OsPPKL1 self-regulates its degradation to orchestrate brassinosteroid signaling in rice.Plant communications · 2024Article
- Advancements in Rice Leaf Development Research.Plants (Basel, Switzerland) · 2024Review
- The osmotic stress-activated receptor-like kinase DPY1 mediates SnRK2 kinase activation and drought tolerance in Setaria.The Plant cell · 2023Article
- Salicylic acid attenuates brassinosteroid signaling via protein de-S-acylation.The EMBO journal · 2023Article
- The putative myristoylome of Physcomitrium patens reveals conserved features of myristoylation in basal land plants.Plant cell reports · 2023Article
- Crosstalk between brassinosteroid signaling and variable nutrient environments.Science China. Life sciences · 2023Review
- The U-box ubiquitin ligase TUD1 promotes brassinosteroid-induced GSK2 degradation in rice.Plant communications · 2023Article
- Comprehensive Analysis of BR Receptor Expression under Hormone Treatment in the Rubber Tree (Plants (Basel, Switzerland) · 2023Article
- Genetic Localization and Homologous Genes Mining for Barley Grain Size.International journal of molecular sciences · 2023Review
1 more citing papers are in PubMed but not listed here.
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13 authors.
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Abstract
Many plant receptor kinases transduce signals through receptor-like cytoplasmic kinases (RLCKs); however, the molecular mechanisms that create an effective on-off switch are unknown. The receptor kinase BR INSENSITIVE1 (BRI1) transduces brassinosteroid (BR) signal by phosphorylating members of the BR-signaling kinase (BSK) family of RLCKs, which contain a kinase domain and a C-terminal tetratricopeptide repeat (TPR) domain. Here, we show that the BR signaling function of BSKs is conserved in Arabidopsis (Arabidopsis thaliana) and rice (Oryza sativa) and that the TPR domain of BSKs functions as a "phospho-switchable" autoregulatory domain to control BSKs' activity. Genetic studies revealed that OsBSK3 is a positive regulator of BR signaling in rice, while in vivo and in vitro assays demonstrated that OsBRI1 interacts directly with and phosphorylates OsBSK3. The TPR domain of OsBSK3, which interacts directly with the protein's kinase domain, serves as an autoinhibitory domain to prevent OsBSK3 from interacting with bri1-SUPPRESSOR1 (BSU1). Phosphorylation of OsBSK3 by OsBRI1 disrupts the interaction between its TPR and kinase domains, thereby increasing the binding between OsBSK3's kinase domain and BSU1. Our results not only demonstrate that OsBSK3 plays a conserved role in regulating BR signaling in rice, but also provide insight into the molecular mechanism by which BSK family proteins are inhibited under basal conditions but switched on by the upstream receptor kinase BRI1.
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