Research ArticleDNA damage

Casein kinase 2 (CK2) phosphorylates the deubiquitylase OTUB1 at Ser16 to trigger its nuclear localization

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Science Signaling  14 Apr 2015:
Vol. 8, Issue 372, pp. ra35
DOI: 10.1126/scisignal.aaa0441

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Sending OTUB1 to the nucleus for DNA damage repair

Without the ability to repair DNA damage, genomic instability occurs, which can lead to cell death or cancer. OTUB1 is an enzyme that either removes ubiquitin that has been covalently attached to target proteins or prevents protein ubiquitylation by inhibiting ubiquitin-conjugating enzymes and functions in both the cytosol and nucleus. In the nucleus, OTUB1 functions in DNA repair. Herhaus et al. found that the kinase CK2 phosphorylated OTUB1, enabling its nuclear translocation in cells. Mutating the CK2 phosphorylation site on OTUB1 or pharmacologically inhibiting CK2 impaired DNA repair in cells exposed to ionizing radiation, which causes DNA damage and is used therapeutically to kill cancer cells. These findings may be exploited to decrease a cancer cell’s ability to tolerate radiation therapy.

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