ArticlePlant molecular biology2025
Structural insights into the recognition of RALF peptides by FERONIA receptor kinase during Brassicaceae pollination.
Article in Plant molecular biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Root development progression involves RALF peptide-mediated ROS signaling and pectin dynamics in rice.Nature communications · 2026Article
- Characterization of self-incompatibility genes inFrontiers in plant science · 2026Article
- Characterization of long non-coding RNAs during compatible and incompatible pollination inFrontiers in plant science · 2026Article
- The RALF-FERONIA Signaling Axis: A Central Hub Integrating Plant Growth, Reproduction, and Stress Responses.International journal of molecular sciences · 2025Review
- Molecular mechanisms and genetic regulation of self-incompatibility in flowering plants: implications for crop improvement and evolutionary biology.Plant molecular biology · 2025Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Ensuring species integrity and successful reproduction is pivotal for the survival of angiosperms. Members of Brassicaceae family employ a "lock and key" mechanism involving stigmatic (sRALFs) and pollen RALFs (pRALFs) binding to FERONIA, a Catharanthus roseus receptor-like kinase 1-like (CrRLK1L) receptor, to establish a prezygotic hybridization barrier. In the absence of compatible pRALFs, sRALFs bind to FERONIA, inducing a lock state for pollen tube penetration. Conversely, compatible pRALFs act as a key, facilitating successful fertilization. Competing pRALFs reduce the sRALFs binding to FERONIA in a dose-dependent manner, enabling pollen tube penetration. Despite its crucial role in Brassicaceae hybridization, the structural basis of this binding remains elusive owing to the highly flexible nature of RALF peptides. Using advanced structural modeling techniques and flexible peptide molecular docking, this study reveals that pRALFs and sRALFs bind to negatively charged pockets in FERONIA with varying binding affinities. Our study unveils the structural basis of this binding, shedding light on the molecular mechanism underlying hybridization barriers in Brassicaceae.
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Registered trials
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