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Fig. 4. Phosphorylation of β2-adaptin by Src reduces its ability to bind β-arrestins. (A) GST-fusion proteins of the ear domain of β2-adaptin were left unphosphorylated (–) or phosphorylated (+) in vitro with purified Src. The amounts of GST-β2-adaptin were assessed by Ponceau Red, and Src-phosphorylated proteins were detected by western blot using anti-phosphotyrosine antibody 4G10 (P-Tyr). (B) After removing Src from the reaction, the unphosphorylated or phosphorylated GST-proteins were incubated with increasing amounts of Flag-β-arrestin1 or 2 from cell lysates. The amounts of β-arrestin associated with the GST-proteins were determined by western blot using an anti-Flag antibody. Whole cell extracts (Total, right panels) were also blotted for detecting the level of Flag-β-arrestin1 or 2 expression using the anti-Flag antibody. Data are representative of three to five independent experiments.
