ArticleProceedings of the National Academy of Sciences of the United States of America2022
Robust designation of meiotic crossover sites by CDK-2 through phosphorylation of the MutSγ complex.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 30 citations in OpenAlex.
- The mid-pachytene transition between early and late double-strand breaks in C. elegans meiosis is conserved throughout early adulthood and coincides with a peak in recombination intermediates.G3 (Bethesda, Md.) · 2026Article
- A mammalian-specific domain of MSH5 drives the transition from crossover licensing to designation during meiotic prophase I.bioRxiv : the preprint server for biology · 2026Article
- Ubiquitin-proteasome system regulates pro-crossover protein dynamics during meiosis in Caenorhabditis elegans.PLoS biology · 2026Article
- Disordered protein COSA-2 maintains crossover-specific repair compartments to ensure meiotic crossover maturation.bioRxiv : the preprint server for biology · 2026Article
- COSA-1-SLX-4 interaction directly links crossover designation with Holliday junction resolution.Science advances · 2026Article
- Forceful Beginnings: Mechanotransduction and Mechanosensation at the Meiotic Cell Nucleus During Gamete Development.Results and problems in cell differentiation · 2026Review
- Multi-step implementation of meiotic crossover patterning.bioRxiv : the preprint server for biology · 2025Article
- Loss of meiotic double strand breaks triggers recruitment of recombination-independent pro-crossover factors in C. elegans spermatogenesis.PLoS genetics · 2025Article
- CNTD1 is crucial for crossover formation in female meiosis and for establishing the ovarian reserve.The Journal of cell biology · 2025Article
- Crossover patterning through condensation and coarsening of pro-crossover factors.Nature cell biology · 2025Article
- Article
- The conserved ATPase PCH-2 controls the number and distribution of crossovers by antagonizing their formation inbioRxiv : the preprint server for biology · 2024Article
- CDK phosphorylation of Sfr1 downregulates Rad51 function in late-meiotic homolog invasions.The EMBO journal · 2024Article
- 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
- COSA-1 mediated pro-crossover complex formation promotes meiotic crossing over in C. elegans.Nucleic acids research · 2024Article
- Article
- Control of meiotic crossover interference by a proteolytic chaperone network.Nature plants · 2024Article
- Centromere-Proximal Suppression of Meiotic Crossovers inbioRxiv : the preprint server for biology · 2023Article
- Caenorhabditis elegans NSE3 homolog (MAGE-1) is involved in genome stability and acts in inter-sister recombination during meiosis.Genetics · 2023Article
- The regulation of meiotic crossover distribution: a coarse solution to a century-old mystery?Biochemical Society transactions · 2023Review
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Authors and funding
9 authors at 3 institutions in 1 country.
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Abstract
Crossover formation is essential for proper segregation of homologous chromosomes during meiosis. Here, we show that Caenorhabditis elegans cyclin-dependent kinase 2 (CDK-2) partners with cyclin-like protein COSA-1 to promote crossover formation by promoting conversion of meiotic double-strand breaks into crossover–specific recombination intermediates. Further, we identify MutSγ component MSH-5 as a CDK-2 phosphorylation target. MSH-5 has a disordered C-terminal tail that contains 13 potential CDK phosphosites and is required to concentrate crossover–promoting proteins at recombination sites. Phosphorylation of the MSH-5 tail appears dispensable in a wild-type background, but when MutSγ activity is partially compromised, crossover formation and retention of COSA-1 at recombination sites are exquisitely sensitive to phosphosite loss. Our data support a model in which robustness of crossover designation reflects a positive feedback mechanism involving CDK-2–mediated phosphorylation and scaffold-like properties of the MSH5 C-terminal tail, features that combine to promote full recruitment and activity of crossover–promoting complexes.
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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.