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The T450 phosphorylation site was mutated to alanine (S473A) or aspartate (S473D) in both myristylated and wild-type constructs. Akt phosphorylation and the downstream targets, GSK3β and S6 ribosomal protein are shown. Actin was used as a loading control, and HA is used to detect the overexpressed constructs. The S473D mutation significantly enhances transformation by both the wild-type and myristylated constructs.
