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. 2015 Apr 29;10(5):373–383. doi: 10.1080/15592294.2015.1028708

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© 2015 The Author(s). Published with license by Taylor & Francis Group, LLC

© Marcella Salzano, Marta Sanz-García, Diana M Monsalve, David S Moura, and Pedro A Lazo

This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.

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Figure 3. — Effect of ionizing radiation on histone phosphorylation. (A) Endogenous VRK1 activated by IR phosphorylates H2AX (left panel) and H3 (right panel). Endogenous VRK1 was immunoprecipitated from A549 or MCF-7 cells. A control immunoprecipitation was carried out with αAU5 antibody. The immunoprecipitated VRK1 was used in an in vitro kinase assay using as substrate recombinant H2AX (left) or H3 (right). (B) Specifity of H2AX phosphorylation by VRK1 induced by IR. To demonstrate the specifity of H2AX phosphorylation, A549 cells were transfected with siRNA control (siCt) or siRNA for VRK1 (siV1-02).VRK1 was immunoprecipitated and used in a kinase assay. Expression of VRK1 is shown at the bottom and γH2AX phosphorylation was evaluated by immunoblots after histone acidic extraction with a phospho-specific antibody.