A B56gamma mutation in lung cancer disrupts the p53-dependent tumor-suppressor function of protein phosphatase 2A.

ABSTRACT: Earlier studies have shown both p53-dependent and -independent tumor-suppressive functions of B56gamma-specific protein phosphatase 2A (B56gamma-PP2A). In the absence of p53, B56gamma-PP2A can inhibit cell proliferation and cell transformation by an unknown mechanism. In the presence of p53, on DNA damage, a complex including B56gamma-PP2A and p53 is formed, which leads to Thr55 dephosphorylation of p53, induction of the p53 transcriptional target p21 and inhibition of cell proliferation. In spite of its significance in inhibition of cell proliferation, no B56gamma mutations have been linked to human cancer to date. In this study, we first differentiate between the p53-dependent and -independent functions of B56gamma-PP2A by identifying a domain of the B56gamma protein required for interac

SUBMITTER: Shouse GP 

PROVIDER: S-EPMC2900437 | biostudies-literature | 2010 Jul

REPOSITORIES: biostudies-literature