Activation of the SUMO modification system is required for the accumulation of RAD51 at sites of DNA damage

Hiroki Shima, Hidekazu Suzuki, Jiying Sun, Kazuteru Kono, Lin Shi, Aiko Kinomura, Yasunori Horikoshi, Tsuyoshi Ikura, Masae Ikura, Roland Kanaar, Kazuhiko Igarashi, Hisato Saitoh, Hitoshi Kurumizaka, Satoshi Tashiro*

*この研究の対応する著者

    研究成果: Article査読

    44 被引用数 (Scopus)

    抄録

    Genetic information encoded in chromosomal DNA is challenged by intrinsic and exogenous sources of DNA damage. DNA doublestrand breaks (DSBs) are extremely dangerous DNA lesions. RAD51 plays a central role in homologous DSB repair, by facilitating the recombination of damaged DNA with intact DNA in eukaryotes. RAD51 accumulates at sites containing DNA damage to form nuclear foci. However, the mechanism of RAD51 accumulation at sites of DNA damage is still unclear. Post-translational modifications of proteins, such as phosphorylation, acetylation and ubiquitylation play a role in the regulation of protein localization and dynamics. Recently, the covalent binding of small ubiquitin-like modifier (SUMO) proteins to target proteins, termed SUMOylation, at sites containing DNA damage has been shown to play a role in the regulation of the DNA-damage response. Here, we show that the SUMOylation E2 ligase UBC9, and E3 ligases PIAS1 and PIAS4, are required for RAD51 accretion at sites containing DNA damage in human cells. Moreover, we identified a SUMO-interacting motif (SIM) in RAD51, which is necessary for accumulation of RAD51 at sites of DNA damage. These findings suggest that the SUMO-SIM system plays an important role in DNA repair, through the regulation of RAD51 dynamics.

    本文言語English
    ページ(範囲)5284-5292
    ページ数9
    ジャーナルJournal of Cell Science
    126
    22
    DOI
    出版ステータスPublished - 2013 11 15

    ASJC Scopus subject areas

    • 細胞生物学

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