ArticleNature plants2025
The synaptonemal complex central element SCEP3 interlinks synapsis initiation and crossover formation in Arabidopsis thaliana.
Article in Nature plants, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- The meiotic achilles' heel: vulnerability and resilience under environmental stress.Protoplasma · 2026Review
- Crossover control: A key to unlocking genetic diversity in plant breeding.Journal of integrative plant biology · 2026Review
- Structure and function of the synaptonemal complex.The Journal of cell biology · 2026Review
- ZSL Orchestrates Synaptonemal Complex Assembly as a Central Region Scaffold to Ensure Synapsis Fidelity and Crossover Control in Polyploid Meiosis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Genomic introgressions from wild relatives in the wheat genome alter meiotic dynamics in inter-varietal hybrids.The Plant journal : for cell and molecular biology · 2026Article
- SCEP3 initiates synapsis and implements crossover interference in Arabidopsis.Nature plants · 2025Article
- Multiple Autopolyploid Arabidopsis lyrata Populations Stabilized by Long-Range Adaptive Introgression Across Eurasia.Molecular biology and evolution · 2025Article
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Authors and funding
13 authors.
Funding
Abstract
The synaptonemal complex (SC) forms between homologous chromosomes during meiosis. In Arabidopsis thaliana, its central region (CR) is composed of the transverse filament protein ZYP1 and the central element proteins SCEP1 and SCEP2. Here we identify SCEP3 as a CR protein that is evolutionarily conserved across plant species. SCEP3 spatiotemporally overlaps with other CR proteins and localizes to the SC CR. The loss of SCEP3 prevents SC assembly, abolishes crossover (CO) assurance and interference, and eliminates sex-specific differences in CO rates (heterochiasmy) through increased CO in females. SCEP3 is required for a subset of COs in SC-deficient mutants, such as zyp1. Although SCEP3 physically interacts with ZYP1, it loads independently of other CR proteins. We propose that SCEP3 may associate with certain recombination intermediates, stabilizing them and/or recruiting additional factors, such as ZYP1, to a subset of these intermediates, thereby promoting and interlinking SC assembly and CO formation.
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