ArticleNature plants2025
Identification of the cytoplasmic motor-LINC complex involved in rapid chromosome movements during meiotic prophase 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.
- Nuclear envelope buffering of cytoskeletal force stabilizes chromosome interactions inbioRxiv : the preprint server for biology · 2026Article
- The HORMA-domain protein ASY1 recruits the plant-specific cyclin SDS to promote DMC1-mediated meiotic recombination.The Plant cell · 2026Article
- Rapid chromosome movements persist within nuclear protrusions in Arabidopsis thaliana meiocytes.Protoplasma · 2026Article
- 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
- Chromosome movements in meiotic prophase: regulatory mechanisms and biological roles.Frontiers in cell and developmental biology · 2026Review
- Forceful Beginnings: Mechanotransduction and Mechanosensation at the Meiotic Cell Nucleus During Gamete Development.Results and problems in cell differentiation · 2026Review
- SCEP3 initiates synapsis and implements crossover interference in Arabidopsis.Nature plants · 2025Article
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Authors and funding
17 authors.
Funding
Abstract
Homologous pairing and recombination during meiosis are facilitated by rapid prophase movements (RPMs), which depend on chromosome attachment to the nuclear envelope (NE) and on cytoplasmic forces transmitted to the chromosomes through the NE, mediated by Linker of Nucleoskeleton and Cytoskeleton (LINC) complexes. In plants, only the NE-associated SUN-domain proteins SUN1 and SUN2 have been identified as components of the RPM process. Here we show that, during meiosis, SUN1 and SUN2 form a LINC complex with the KASH-domain protein SINE3, which recruits the meiosis-specific kinesin PSS1 to the NE. These proteins accumulate at telomere-binding sites in the NE, and their loss disrupts telomere attachment and bouquet formation and abolishes RPMs. These defects lead to defective synapsis and clustered crossovers, resulting in chromosome mis-segregation. Our results establish that the mechanism underlying RPMs is conserved in Arabidopsis thaliana, with RPMs primarily facilitating homologous recognition rather than preventing non-homologous interactions.
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