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Cell Cycle. 2012 Feb 1;11(3):604-16. doi: 10.4161/cc.11.3.19114. Epub 2012 Feb 1.

Cyclin G-associated kinase regulates protein phosphatase 2A by phosphorylation of its B'γ subunit.

Author information

1
Department of Molecular Genetics, Research Institute for Microbial Diseases, Osaka University, Suita City, Osaka, Japan.

Abstract

Protein phosphatase 2A (PP2A) bearing the B'γ (=B'α/B56γ1/PR61γ) subunit is recruited to dephosphorylation targets by cyclin G. We demonstrate here that cyclin G-associated kinase (GAK), a component of the GAK/B'γ/cyclin G complex, directly phosphorylates the B'γ-Thr104 residue and regulates PP2A activity. Indeed, an anti-B'γ-pT104 antibody detected immunofluorescence signals at the chromosome and centrosome during mitosis; these signals were reduced by siRNA-mediated GAK knockdown. After DNA damage by γ-irradiation, the chromosome signals formed foci that colocalized with a DNA double-strand break (DSB) marker H2AX-pS139 (γH2AX) and CHK2-pT68. Moreover, B'γ-pT104 enhanced PP2A holoenzyme assembly and PP2A activity, as shown by the results of an in vitro phosphatase assay. These results suggest a novel role for GAK as a regulator of dephosphorylation events under the control of the PP2A B'γ subunit.

PMID:
22262175
DOI:
10.4161/cc.11.3.19114
[Indexed for MEDLINE]

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