Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 286, Issue 13, Pages 10911-10917Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.C110.210211
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Funding
- National Institutes of Health [CA129325]
- Massey University
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The p53 tumor suppressor is principally regulated by post-translational modifications and proteasome-dependent degradation. Various kinases have been shown to phosphorylate p53, but little is known about the counteracting phosphatases. We demonstrate here that the newly identified complex GAS41-PP2C beta, and not PP2C beta alone, is specifically required for dephosphorylation of serine 366 on p53. Ectopic expression of GAS41 and PP2C beta reduces UV radiation-induced p53 up-regulation, thereby increasing the cell survival upon genotoxic DNA damage. To our knowledge, the GAS41-PP2C beta complex is the first example in which substrate specificity of a PP2C family member is controlled by an associated regulatory subunit. Because GAS41 is frequently amplified in human gliomas, our finding illustrates a novel oncogenic mechanism of GAS41 by p53 dephosphorylation.
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