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Figure 2


Fig. 2. Met triggers translation of Mdm2 in cultured embryonic hepatocytes without affecting protein stability. (A) Time-course analysis of Mdm2 protein levels upon Hgf stimulation. Total extracts from wild-type embryonic hepatocytes were blotted and probed with {alpha}-Mdm2 (top) and {alpha}-tubulin (bottom). (B) Levels of newly synthesized Mdm2 in {alpha}-Mdm2 immunoprecipitates (top panel) of 35S-methionine/cysteine labeled embryonic hepatocytes treated or not with Hgf (H). The middle and lower panels show levels of Mdm2 and tubulin, respectively, on total lysates. (C) Rate of decay of Mdm2 protein in embryonic hepatocytes with high Mdm2 levels (Hgf stimulation for 24 hours; top panel) as determined by cycloheximide (CHX) treatment. Hgf treatment (H) does not change Mdm2 protein stability. CHX does not affect the half-life of tubulin. The decrease in Mdm2 protein levels was quantified after normalization with tubulin (bottom panel).





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