Protein kinase CK2 localizes to sites of DNA double-strand break regulating the cellular response to DNA damage.

ABSTRACT:

Background

The DNA-dependent protein kinase (DNA-PK) is a nuclear complex composed of a large catalytic subunit (DNA-PKcs) and a heterodimeric DNA-targeting subunit Ku. DNA-PK is a major component of the non-homologous end-joining (NHEJ) repair mechanism, which is activated in the presence of DNA double-strand breaks induced by ionizing radiation, reactive oxygen species and radiomimetic drugs. We have recently reported that down-regulation of protein kinase CK2 by siRNA interference results in enhanced cell death specifically in DNA-PKcs-proficient human glioblastoma cells, and this event is accompanied by decreased autophosphorylation of DNA-PKcs at S2056 and delayed repair of DNA double-strand breaks.

Results

In the present study, we show that CK2 co-localizes with phosph

SUBMITTER: Olsen BB 

PROVIDER: S-EPMC3316135 | biostudies-literature | 2012 Mar

REPOSITORIES: biostudies-literature