Cyclin G recruits PP2A to dephosphorylate Mdm2 |
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Authors: | Okamoto Koji Li Hongyun Jensen Michael R Zhang Tingting Taya Yoichi Thorgeirsson Snorri S Prives Carol |
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Institution: | Department of Biological Sciences, Columbia University, New York, NY 10027, USA. |
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Abstract: | The function of cyclin G, a commonly induced p53 target, has remained elusive. We show that cyclin G forms a quaternary complex in vivo and in vitro with enzymatically active phosphatase 2A (PP2A) holoenzymes containing B' subunits. Interestingly, cyclin G also binds in vivo and in vitro to Mdm2 and markedly stimulates the ability of PP2A to dephosphorylate Mdm2 at T216. Consistent with these data, cyclin G null cells have both Mdm2 that is hyperphosphorylated at T216 and markedly higher levels of p53 protein when compared to wild-type cells. Cyclin G expression also results in reduced phosphorylation of human Hdm2 at S166. Thus, our data suggest that cyclin G recruits PP2A in order to modulate the phosphorylation of Mdm2 and thereby to regulate both Mdm2 and p53. |
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