ArticleThe Plant cell2007
Characterization of the SP11/SCR high-affinity binding site involved in self/nonself recognition in brassica self-incompatibility.
Article in The Plant cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 104 citations in OpenAlex.
- Deciphering the Transcriptomic Dynamics of Self-Incompatibility in Yellow Passion Fruit: Evidence of Modified Sporophytic Mechanism.Plants (Basel, Switzerland) · 2026Article
- Several plant self-incompatibility systems may be controlled by atypical receptor-ligand interactions.The Plant journal : for cell and molecular biology · 2026Review
- From recognition to response: integrated signaling pathways determining pollen acceptance and rejection in Brassicaceae.The New phytologist · 2026Review
- Insights into the Molecular Basis of Pollen Coat Development and Its Role in Male Sterility.International journal of molecular sciences · 2025Review
- Nontransformation methods for studying signaling pathways and genes involved in Brassica rapa pollen-stigma interactions.Plant physiology · 2024Article
- Involvement of CgHSFB1 in the regulation of self-incompatibility in 'Shatian' pummelo.Plant molecular biology · 2024Article
- A pollen selection system links self and interspecific incompatibility in the Brassicaceae.Nature ecology & evolution · 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
- MLPK function is not required for self-incompatibility in the SPlant reproduction · 2023Article
- Paradigms of receptor kinase signaling in plants.The Biochemical journal · 2023Review
- Insights into pollen-stigma recognition: self-incompatibility mechanisms serve as interspecies barriers in Brassicaceae?aBIOTECH · 2023Article
- 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
- Genetic Diversity of Genes Controlling Unilateral Incompatibility in Japanese Cultivars of Chinese Cabbage.Plants (Basel, Switzerland) · 2021Article
- Expression of Brassica napus GLO1 is sufficient to breakdown artificial self-incompatibility in Arabidopsis thaliana.Plant reproduction · 2020Article
- Mechanism of self/nonself-discrimination in Brassica self-incompatibility.Nature communications · 2020Article
- Fertilization in flowering plants: an odyssey of sperm cell delivery.Plant molecular biology · 2020Review
- Article
- Morphological Type Identification of Self-Incompatibility inInternational journal of molecular sciences · 2018Article
- Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Brassica self-incompatibility, the recognition of self/nonself pollen grains, is controlled by the S-locus, which encodes three highly polymorphic proteins: S-locus receptor kinase (SRK), S-locus protein 11 (SP11; also designated S-locus Cys-rich protein), and S-locus glycoprotein (SLG). SP11, located in the pollen coat, determines pollen S-haplotype specificity, whereas SRK, located on the plasma membrane of stigmatic papilla cells, determines stigmatic S-haplotype specificity. SLG shares significant sequence similarity with the extracellular domain of SRK and is abundant in the stigmatic cell wall, but its function is controversial. We previously showed that SP11 binds directly to its cognate SRK with high affinity (K(d) = 0.7 nM) and induces its autophosphorylation. We also found that an SLG-like, 60-kD protein on the stigmatic membrane forms a high-affinity binding site for SP11. Here, we show that the 60-kD stigmatic membrane protein is a truncated form of SRK containing the extracellular domain, transmembrane domain, and part of the juxtamembrane domain. A transiently expressed, membrane-anchored form of SRK exhibits high-affinity binding to SP11, whereas the soluble SRK (eSRK) lacking the transmembrane domain exhibits no high-affinity binding, as is the case with SLG. The different binding affinities of the membrane-anchored SRK and soluble eSRK or SLG will be significant for the specific perception of SP11 by SRK.
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