The proteinaceous zipper-like structure known as the synaptonemal complex (SC), which forms between pairs of homologous chromosomes during meiosis from yeast to humans, plays important roles in promoting interhomolog crossover formation, regulating cessation of DNA double-strand break (DSB) formation following crossover designation, and ensuring accurate meiotic chromosome segregation. Recent studies are starting to reveal critical roles for different protein modifications in regulating SC dynamics. Protein SUMOylation, N-terminal acetylation, and phosphorylation have been shown to be essential for the regulated assembly and disassembly of the SC. Moreover, phosphorylation of specific SC components has been found to link changes in SC dynamics with meiotic recombination. This review highlights the latest findings on how protein modifications regulate SC dynamics and functions.

在从酵母到人的减数分裂过程中，在成对的同源染色体之间形成的称为突触复合物（SC）的蛋白状拉链状结构，在促进同源性交叉形成，调节DNA双链断裂（DSB）形成的停止中起重要作用。交叉指定后，确保准确的减数分裂染色体分离。最近的研究开始揭示不同蛋白质修饰在调节SC动态中的关键作用。蛋白质SUMOylation，N-末端乙酰化和磷酸化已被证明对于调控SC的组装和拆卸至关重要。而且，已经发现特定SC组分的磷酸化将SC动力学的变化与减数分裂重组联系起来。