| Literature DB >> 29290403 |
Jinmin Gao1, Monica P Colaiácovo2.
Abstract
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.Entities:
Keywords: N-terminal acetylation; SUMOylation; meiosis; meiotic recombination; phosphorylation; synaptonemal complex
Mesh：
Year: 2017 PMID： 29290403 PMCID： PMC5834363 DOI： 10.1016/j.tig.2017.12.001
Source DB: PubMed Journal: Trends Genet ISSN： 0168-9525 Impact factor: 11.639