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Kao, G.D. et al.

Kao, McKenna, Guenther, Muschel, Lazar, Yen,

Histone deacetylase 4 interacts with 53BP1 to mediate the DNA damage response.

Anumber of proteins are recruited to nuclear foci upon exposure to double-strand DNA damage, including 53BP1 and Rad51, but the precise role of these DNA damage-induced foci remain unclear. Here we show in a variety of human cell lines that histone deacetylase (HDAC) 4 is recruited to foci with kinetics similar to, and colocalizes with, 53BP1 after exposure to agents causing double-stranded DNA breaks. HDAC4 foci gradually disappeared in repair-proficient cells but persisted in repair-deficient cell lines or cells irradiated with a lethal dose, suggesting that resolution of HDAC4 foci is linked to repair. Silencing of HDAC4 via RNA interference surprisingly also decreased levels of 53BP1 protein, abrogated the DNA damage-induced G2 delay, and radiosensitized HeLa cells. Our combined results suggest that HDAC4 is a critical component of the DNA damage response pathway that acts through 53BP1 and perhaps contributes in maintaining the G2 cell cycle checkpoint.[1]

References

Histone deacetylase 4 interacts with 53BP1 to mediate the DNA damage response. Kao, G.D., McKenna, W.G., Guenther, M.G., Muschel, R.J., Lazar, M.A., Yen, T.J. J. Cell Biol. (2003) [Pubmed]

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