ArticleGenes & development2022
The Zip4 protein directly couples meiotic crossover formation to synaptonemal complex assembly.
Article in Genes & development, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 48 citations in OpenAlex.
- Cohesin release-factor Wapl modulates axis and chromatin structure to promote conjunction and separation of meiotic chromosomes.Cell reports · 2026Article
- Crossover formation and coordinated assembly of synaptonemal complex relies on a direct interaction between Zip1 and Zip3.Genetics · 2026Article
- Structure and function of the synaptonemal complex.The Journal of cell biology · 2026Review
- RPA directly stimulates Mer3 helicase processivity to ensure normal crossover formation in meiosis.Nature communications · 2026Article
- Mms4 chromosomal association reveals functional relationships between meiotic crossover pathways in budding yeast.PLoS genetics · 2026Article
- Ufd2p promotes efficient crossover formation by destabilizing Top2p during meiosis.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Article
- The conserved SEN1 DNA/RNA helicase has multiple functions during yeast meiosis.PLoS genetics · 2025Article
- Article
- Rad51, Rad54, and ZMM proteins antagonize the mismatch repair system to promote fertility of budding yeast intraspecies hybrid zygotes.Nucleic acids research · 2025Article
- UBE2J2 is essential for the progression of meiosis prophase I during spermatogenesis in mice.iScience · 2025Article
- The synaptonemal complex central element SCEP3 interlinks synapsis initiation and crossover formation in Arabidopsis thaliana.Nature plants · 2025Article
- Genetic dissection of MutL complexes in Arabidopsis meiosis.Nucleic acids research · 2025Article
- Proximity labeling reveals new functional relationships between meiotic recombination proteins in S. cerevisiae.PLoS genetics · 2024Article
- DNA cytosine methyltransferases differentially regulate genome-wide hypermutation and interhomolog recombination in Trichoderma reesei meiosis.Nucleic acids research · 2024Article
- Canonical and noncanonical roles of Hop1 are crucial for meiotic prophase in the fungus Sordaria macrospora.PLoS biology · 2024Article
- Formation and resolution of meiotic chromosome entanglements and interlocks.Journal of cell science · 2024Review
- RNF212B E3 ligase is essential for crossover designation and maturation during male and female meiosis in the mouse.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The molecular machinery of meiotic recombination.Biochemical Society transactions · 2024Review
- Skp1 proteins are structural components of the synaptonemal complex inScience advances · 2024Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Meiotic recombination is triggered by programmed double-strand breaks (DSBs), a subset of these being repaired as crossovers, promoted by eight evolutionarily conserved proteins, named ZMM. Crossover formation is functionally linked to synaptonemal complex (SC) assembly between homologous chromosomes, but the underlying mechanism is unknown. Here we show that Ecm11, a SC central element protein, localizes on both DSB sites and sites that attach chromatin loops to the chromosome axis, which are the starting points of SC formation, in a way that strictly requires the ZMM protein Zip4. Furthermore, Zip4 directly interacts with Ecm11, and point mutants that specifically abolish this interaction lose Ecm11 binding to chromosomes and exhibit defective SC assembly. This can be partially rescued by artificially tethering interaction-defective Ecm11 to Zip4. Mechanistically, this direct connection ensuring SC assembly from CO sites could be a way for the meiotic cell to shut down further DSB formation once enough recombination sites have been selected for crossovers, thereby preventing excess crossovers. Finally, the mammalian ortholog of Zip4, TEX11, also interacts with the SC central element TEX12, suggesting a general mechanism.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.