Format

Send to

Choose Destination
Trends Genet. 2018 Mar;34(3):232-245. doi: 10.1016/j.tig.2017.12.001. Epub 2017 Dec 28.

Zipping and Unzipping: Protein Modifications Regulating Synaptonemal Complex Dynamics.

Author information

1
Institute of Biomedical Sciences, College of Life Sciences, Key Laboratory of Animal Resistance Biology of Shandong Province, Shandong Normal University, Jinan, Shandong, 250014, China; Department of Genetics, Harvard Medical School, Boston, MA 02115, USA.
2
Department of Genetics, Harvard Medical School, Boston, MA 02115, USA. Electronic address: mcolaiacovo@genetics.med.harvard.edu.

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.

KEYWORDS:

N-terminal acetylation; SUMOylation; meiosis; meiotic recombination; phosphorylation; synaptonemal complex

PMID:
29290403
PMCID:
PMC5834363
DOI:
10.1016/j.tig.2017.12.001
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Elsevier Science Icon for PubMed Central
Loading ...
Support Center