ArticleCell research2016
Structural basis for specific self-incompatibility response in Brassica.
Article in Cell research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- Disulfide-bond-driven neck-ring-like conformation mediates SCREW recognition in plant immunity.Nature plants · 2026Article
- Cross incompatibility restricting genome exchange and diversification of primary gene pool in plants: challenges and opportunities.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2026Review
- From recognition to response: integrated signaling pathways determining pollen acceptance and rejection in Brassicaceae.The New phytologist · 2026Review
- Several plant self-incompatibility systems may be controlled by atypical receptor-ligand interactions.The Plant journal : for cell and molecular biology · 2026Review
- Plant cell surface receptors.The Plant journal : for cell and molecular biology · 2026Review
- Pan-family pollen signals control an interspecific stigma barrier across Brassicaceae species.Science (New York, N.Y.) · 2026Article
- Characterization of self-incompatibility genes inFrontiers in plant science · 2026Article
- Molecular mechanisms and genetic regulation of self-incompatibility in flowering plants: implications for crop improvement and evolutionary biology.Plant molecular biology · 2025Review
- Nontransformation methods for studying signaling pathways and genes involved in Brassica rapa pollen-stigma interactions.Plant physiology · 2024Article
- Self-incompatibility phenotypes of SRK mutants can be predicted with high accuracy.bioRxiv : the preprint server for biology · 2024Article
- Molecular mechanisms of self-incompatibility in Brassicaceae and Solanaceae.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2024Review
- Stop and go signals at the stigma-pollen interface of the Brassicaceae.Plant physiology · 2023Article
- Self-incompatibility: a targeted, unexplored pre-fertilization barrier in flower crops of Asteraceae.Journal of plant research · 2023Review
- Paradigms of receptor kinase signaling in plants.The Biochemical journal · 2023Review
- Ancestral self-compatibility facilitates the establishment of allopolyploids in Brassicaceae.Plant reproduction · 2023Review
- Article
- Comprehensive computational analysis of the SRK-SP11 molecular interaction underlying self-incompatibility in Brassicaceae using improved structure prediction for cysteine-rich proteins.Computational and structural biotechnology journal · 2023Article
- Molecular plant immunity against biotrophic, hemibiotrophic, and necrotrophic fungi.Essays in biochemistry · 2022Review
- A pair of non-Mendelian genes at the Ga2 locus confer unilateral cross-incompatibility in maize.Nature communications · 2022Article
- Identification of the genes atFrontiers in plant science · 2022Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Self-incompatibility (SI) is a widespread mechanism in flowering plants which prevents self-fertilization and inbreeding. In Brassica, recognition of the highly polymorphic S-locus cysteine-rich protein (SCR; or S-locus protein 11) by the similarly polymorphic S-locus receptor kinase (SRK) dictates the SI specificity. Here, we report the crystal structure of the extracellular domain of SRK9 (eSRK9) in complex with SCR9 from Brassica rapa. SCR9 binding induces eSRK9 homodimerization, forming a 2:2 eSRK:SCR heterotetramer with a shape like the letter "A". Specific recognition of SCR9 is mediated through three hyper-variable (hv) regions of eSRK9. Each SCR9 simultaneously interacts with hvI and one-half of hvII from one eSRK9 monomer and the other half of hvII from the second eSRK9 monomer, playing a major role in mediating SRK9 homodimerization without involving interaction between the two SCR9 molecules. Single mutations of residues critical for the eSRK9-SCR9 interaction disrupt their binding in vitro. Our study rationalizes a body of data on specific recognition of SCR by SRK and provides a structural template for understanding the co-evolution between SRK and SCR.
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