Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.
Skip to main content

The p53 cofactor Strap (stress responsive activator of p300) is directly targeted by the DNA damage signalling pathway where phosphorylation by ATM (ataxia telangiectasia mutated) kinase facilitates nuclear accumulation. Here, we show that Strap regulation reflects the coordinated interplay between different DNA damage-activated protein kinases, ATM and Chk2 (Checkpoint kinase 2), where phosphorylation by each kinase provides a distinct functional consequence on the activity of Strap. ATM phosphorylation prompts nuclear accumulation, which we show occurs by impeding nuclear export, whereas Chk2 phosphorylation augments protein stability once Strap has attained a nuclear location. These results highlight the various functional roles undertaken by the DNA damage signalling kinases in Strap control and, more generally, shed light on the pathways that contribute to the regulation of the p53 response.

Original publication

DOI

10.1038/embor.2008.186

Type

Journal article

Journal

EMBO Rep

Publication Date

12/2008

Volume

9

Pages

1222 - 1229

Keywords

Active Transport, Cell Nucleus, Amino Acid Sequence, Ataxia Telangiectasia Mutated Proteins, Cell Cycle Proteins, Cell Line, Cell Nucleus, Checkpoint Kinase 2, DNA-Binding Proteins, Humans, Molecular Sequence Data, Neoplasm Proteins, Phosphorylation, Protein Stability, Protein-Serine-Threonine Kinases, Tumor Suppressor Protein p53, Tumor Suppressor Proteins