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• W3098551444 abstract "Summary The DNA damage response (DDR) is a highly orchestrated process but how double-strand DNA breaks (DSBs) are initially recognized is unclear. Here, we show that polymerized SIRT6 deacetylase recognizes DSBs and potentiates the DDR. First, SIRT1 deacetylates SIRT6 at residue K33, which is important for SIRT6 polymerization and mobilization toward DSBs. Then, K33-deacetylated SIRT6 anchors to γH2AX, allowing its retention on and subsequent remodeling of local chromatin. We show that a K33R mutation that mimics hypoacetylated SIRT6 can rescue defective DNA repair as a result of SIRT1 deficiency in cultured cells. These data highlight the synergistic action between SIRTs in the spatiotemporal regulation of the DDR and DNA repair." @default.
• W3098551444 created "2020-11-23" @default.
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• W3098551444 date "2020-02-02" @default.
• W3098551444 modified "2023-10-18" @default.
• W3098551444 title "Synergy between SIRT1 and SIRT6 helps recognize DNA breaks and potentiate the DNA damage response and repair" @default.
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• W3098551444 doi "https://doi.org/10.1101/2020.02.01.930172" @default.
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