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• W2067305429 abstract "Neil Hunter and colleagues show that the HEI10 ubiquitin ligase regulates meiotic recombination by limiting the colocalization of RNF212 and MSH4-MSH5 to future crossover sites. At later stages, they find that HEI10 accumulates stably at designated crossover sites and facilitates clearance of RNF212 and MSH4-MSH5 complexes to promote the final steps of meiotic recombination. Crossover recombination facilitates the accurate segregation of homologous chromosomes during meiosis1,2. In mammals, poorly characterized regulatory processes ensure that every pair of chromosomes obtains at least one crossover, even though most recombination sites yield non-crossovers3. Designation of crossovers involves selective localization of the SUMO ligase RNF212 to a minority of recombination sites, where it stabilizes pertinent factors such as MutSγ (ref. 4). Here we show that the ubiquitin ligase HEI10 (also called CCNB1IP1)5,6 is essential for this crossover/non-crossover differentiation process. In HEI10-deficient mice, RNF212 localizes to most recombination sites, and dissociation of both RNF212 and MutSγ from chromosomes is blocked. Consequently, recombination is impeded, and crossing over fails. In wild-type mice, HEI10 accumulates at designated crossover sites, suggesting that it also has a late role in implementing crossing over. As with RNF212, dosage sensitivity for HEI10 indicates that it is a limiting factor for crossing over. We suggest that SUMO and ubiquitin have antagonistic roles during meiotic recombination that are balanced to effect differential stabilization of recombination factors at crossover and non-crossover sites." @default.
• W2067305429 created "2016-06-24" @default.
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• W2067305429 date "2014-01-05" @default.
• W2067305429 modified "2023-10-06" @default.
• W2067305429 title "Antagonistic roles of ubiquitin ligase HEI10 and SUMO ligase RNF212 regulate meiotic recombination" @default.
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• W2067305429 doi "https://doi.org/10.1038/ng.2858" @default.
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