[HTML][HTML] MEK-ERK-mediated phosphorylation of Mdm2 at Ser-166 in hepatocytes: Mdm2 is activated in response to inhibited Akt signaling
Mdm2 inactivates the tumor suppressor p53 and Akt has been shown to be a major activator
of Mdm2 in many cell types. We have investigated the regulation of Mdm2 in hepatocytes.
We found that growth factor-induced Ser-166 phosphorylation of Mdm2 was inhibited by the
MEK inhibitors U0126 and PD98059 in HepG2 cells and in a rat liver cell line, TRL 1215.
Also, bile acids and oxidative stress induced phosphorylation of Mdm2 at Ser-166 by an
apparently MEK-ERK-dependent mechanism. In contrast, Ser-166 phosphorylation of Mdm2 …
of Mdm2 in many cell types. We have investigated the regulation of Mdm2 in hepatocytes.
We found that growth factor-induced Ser-166 phosphorylation of Mdm2 was inhibited by the
MEK inhibitors U0126 and PD98059 in HepG2 cells and in a rat liver cell line, TRL 1215.
Also, bile acids and oxidative stress induced phosphorylation of Mdm2 at Ser-166 by an
apparently MEK-ERK-dependent mechanism. In contrast, Ser-166 phosphorylation of Mdm2 …
