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. Author manuscript; available in PMC: 2009 Sep 22.
Published in final edited form as: Oncogene. 2009 May 18;28(26):2436–2445. doi: 10.1038/onc.2009.98

Figure 5.

Figure 5

Phosphorylation of Akt on the T92- and T450-Pro motifs is critical for the maintenance of Akt stability. (a) Relative Akt protein and phosphorylation levels on the Thr-Pro motifs were measured by anti-Akt antibody, anti-MPM2 antibody, and a phosphospecific antibody against the phosphorylated Thr450-Pro motif of human Akt1 (Akt-pT450). Expression of tubulin in the whole cell lysate (10% of input) was used as an input loading control for the IP. Fold changes of Akt-total and Akt-pS473 levels of each Akt mutant were normalized with that of the levels of wild-type Akt. (b) Cycloheximide chase of exogeneous, HA-tagged wild-type human Akt1 (Akt1-WT), and Akt1-T92A/T450A (Akt1-AA). (c) Quantification of Akt proteins from three independent experiments with cycloheximide chasing. WT, wild-type Akt1; AA, Akt1-T92A/T450A mutant. (d) Basal and IGF-1 stimulated Akt protein and activation phosphorylation at T308 and S473 sites in Pin1 wild type (+/+) or Pin1 (−/−) MEFs.