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Published on: June 9, 2017
ATM and Chk2 kinase target the p53 cofactor Strap
Cassandra J Adams1, Anne L Graham, Martin Jansson
1Laboratory of Cancer Biology, Medical Sciences Division, Department of Clinical Pharmacology, University of Oxford, Oxford OX3 7DQ, UK.
EMBO Reports
|October 4, 2008
Summary
The stress responsive activator of p300 (Strap) cofactor
Area of Science:
- Molecular Biology
- Cellular Signaling
- DNA Damage Response
Background:
- The p53 pathway is crucial for cellular response to DNA damage.
- Strap (stress responsive activator of p300) is a p53 cofactor involved in DNA damage signaling.
- ATM kinase phosphorylates Strap, promoting its nuclear accumulation.
Purpose of the Study:
- To elucidate the distinct roles of ATM and Chk2 kinases in regulating Strap.
- To understand how Strap's function is modulated by DNA damage signaling pathways.
Main Methods:
- Investigated the interplay between ATM, Chk2, and Strap.
- Analyzed the effects of kinase phosphorylation on Strap's nuclear localization and stability.
- Utilized cell-based assays to study DNA damage response pathways.
Main Results:
- ATM phosphorylation of Strap facilitates nuclear accumulation by inhibiting nuclear export.
- Chk2 phosphorylation enhances Strap protein stability within the nucleus.
- Distinct phosphorylation events by ATM and Chk2 impart unique functional consequences on Strap.
Conclusions:
- Strap regulation involves a coordinated action of ATM and Chk2 kinases.
- Differential kinase activity fine-tunes Strap's role in the DNA damage response.
- These findings offer insights into the complex regulation of the p53 pathway.
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