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Alliance"],"published-print":{"date-parts":[[2018,6]]},"abstract":"<jats:p>The synaptonemal complex is a proteinaceous structure essential for meiotic recombination, and its components have been assumed to play a role exclusively in the germ line. However, SYCE2, a component constituting the synaptonemal complex, is expressed at varying levels in somatic cells. Considering its potent protein-binding activities, it may be possible that SYCE2 plays a somatic role by affecting nuclear functions. Here, we show that SYCE2 constitutively insulates HP1\u03b1 from trimethylated histone H3 lysine 9 (H3K9me3) to promote DNA double-strand break repair. Unlike other HP1\u03b1-binding proteins, which use the canonical PXVXL motifs for their bindings, SYCE2 interacts with the chromoshadow domain of HP1\u03b1 through its N-terminal hydrophobic sequence. SYCE2 reduces HP1\u03b1-H3K9me3 binding without affecting H3K9me3 levels and potentiates ataxia telangiectasia mutated\u2013mediated double-strand break repair activity even in the absence of exogenous DNA damage. Such a somatic role of SYCE2 is ubiquitously observed even if its expression levels are low. These findings suggest that SYCE2 plays a somatic role in the link between the nuclear microenvironment and the DNA damage response potentials as a scaffold of HP1\u03b1 localization.<\/jats:p>","DOI":"10.26508\/lsa.201800021","type":"journal-article","created":{"date-parts":[[2018,6,22]],"date-time":"2018-06-22T11:55:12Z","timestamp":1529668512000},"page":"e201800021","update-policy":"https:\/\/doi.org\/10.26508\/lsa.crossmarkpolicy","source":"Crossref","is-referenced-by-count":8,"title":["Somatic role of SYCE2: an insulator that dissociates HP1\u03b1 from H3K9me3 and potentiates DNA 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