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Mol Cell. 2002 Apr;9(4):761-71.

Cyclin G recruits PP2A to dephosphorylate Mdm2.

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1
Department of Biological Sciences, Columbia University, New York, NY 10027, USA.

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.

PMID:
11983168
DOI:
10.1016/s1097-2765(02)00504-x
[Indexed for MEDLINE]
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