ArticlePlant physiology2013
Visualization of BRI1 and BAK1(SERK3) membrane receptor heterooligomers during brassinosteroid signaling.
Article in Plant physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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50 citing papers in PubMed, 127 citations in OpenAlex.
- Distinct domains of ENHANCER OF PINOID hold information for its polarization required for auxin-mediated cotyledon and flower development in Arabidopsis.PLoS genetics · 2025Article
- Brassinosteroid Signaling Dynamics: Ubiquitination-Dependent Regulation of Core Signaling Components.International journal of molecular sciences · 2025Review
- Genome Identification, Expression Profile Analysis, and Abiotic Stress Response Mechanism of LonganInternational journal of molecular sciences · 2025Article
- Mechanistic Insights into the Function of 14-3-3 Proteins as Negative Regulators of Brassinosteroid Signaling in Arabidopsis.Plant & cell physiology · 2024Article
- Physiology and molecular biology of plants : an international journal of functional plant biology · 2024Article
- Macromolecular tool box to elucidate CLAVATA3/EMBRYO SURROUNDING REGION-RELATED-RLK binding, signaling, and downstream effects.Journal of experimental botany · 2024Article
- The cap-binding complex modulates ABA-responsive transcript splicing during germination in barley (Hordeum vulgare).Scientific reports · 2024Article
- Comparison of Root Transcriptomes against Clubroot Disease Pathogens in a Resistant Chinese Cabbage Cultivar (Plants (Basel, Switzerland) · 2024Article
- Guidelines for naming and studying plasma membrane domains in plants.Nature plants · 2024Review
- Genome-wide identification, characterization and gene expression of BES1 transcription factor family in grapevine (Vitis vinifera L.).Scientific reports · 2023Article
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- Moonlighting Proteins Shine New Light on Molecular Signaling Niches.International journal of molecular sciences · 2021Review
- It takes two to tango - molecular links between plant immunity and brassinosteroid signalling.Journal of cell science · 2020Review
- State-of-the-Art Technologies for Understanding Brassinosteroid Signaling Networks.International journal of molecular sciences · 2020Review
- The manifold actions of signaling peptides on subcellular dynamics of a receptor specify stomatal cell fate.eLife · 2020Article
- Genome-wide analysis of brassinosteroid responsive small RNAs in Arabidopsis thaliana.Genes & genomics · 2020Article
- Regulation of Three Key Kinases of Brassinosteroid Signaling Pathway.International journal of molecular sciences · 2020Review
- The Nanoscale Organization of the Plasma Membrane and Its Importance in Signaling: A Proteolipid Perspective.Plant physiology · 2020Review
- Deviating from the Beaten Track: New Twists in Brassinosteroid Receptor Function.International journal of molecular sciences · 2020Review
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10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The leucine-rich repeat receptor-like kinase BRASSINOSTEROID-INSENSITIVE1 (BRI1) is the main ligand-perceiving receptor for brassinosteroids (BRs) in Arabidopsis (Arabidopsis thaliana). Binding of BRs to the ectodomain of plasma membrane (PM)-located BRI1 receptors initiates an intracellular signal transduction cascade that influences various aspects of plant growth and development. Even though the major components of BR signaling have been revealed and the PM was identified as the main site of BRI1 signaling activity, the very first steps of signal transmission are still elusive. Recently, it was shown that the initiation of BR signal transduction requires the interaction of BRI1 with its SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE (SERK) coreceptors. In addition, the resolved structure of the BRI1 ectodomain suggested that BRI1-ASSOCIATED KINASE1 [BAK1](SERK3) may constitute a component of the ligand-perceiving receptor complex. Therefore, we investigated the spatial correlation between BRI1 and BAK1(SERK3) in the natural habitat of both leucine-rich repeat receptor-like kinases using comparative colocalization analysis and fluorescence lifetime imaging microscopy. We show that activation of BR signaling by exogenous ligand application resulted in both elevated colocalization between BRI1 and BAK1(SERK3) and an about 50% increase of receptor heterooligomerization in the PM of live Arabidopsis root epidermal cells. However, large populations of BRI1 and BAK1(SERK3) colocalized independently of BRs. Moreover, we could visualize that approximately 7% of the BRI1 PM pool constitutively heterooligomerizes with BAK1(SERK3) in live root cells. We propose that only small populations of PM-located BRI1 and BAK1(SERK3) receptors participate in active BR signaling and that the initiation of downstream signal transduction involves preassembled BRI1-BAK1(SERK3) heterooligomers.
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