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Figure 4


Fig. 4. The mTOR pathway is activated upon Hgf stimulation and is required for Met-triggered Mdm2 translation in embryonic hepatocytes. (A) Hgf activates mTOR-p70s6k signaling. p70s6k is phosphorylated on T389 upon Hgf stimulation. Because this phosphorylation is abolished in the presence of LY 294002 (5 µM) or rapamycin (rapa: 1 µM), it must require intact PI3K and mTOR signaling. (B) Hgf stimulation induces phosphorylation of the following mTOR downstream signals: p70s6k on residues T421/S424, S6 ribosomal protein on S235/236 and 4EBP1 on S65. (C) Rapamycin prevents the upregulation of Mdm2 by Hgf in embryonic hepatocyte cultures. (D) Newly synthesized Mdm2 and p53 proteins were analyzed by the immunoprecipitation of 35S-methionine/cysteine-labeled protein extracts from embryonic hepatocytes treated or not with Hgf and/or rapamycin. Rapamycin inhibits the translation of Mdm2, but not of p53. The bottom panels show levels of Mdm2 on total lysates.





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