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Fig. 4 | Cellular & Molecular Biology Letters

Fig. 4

From: Effect of the glycine-rich domain in GAREM2 on its unique subcellular localization upon EGF stimulation

Fig. 4

Effects of glycine-rich domain (GRD) in GAREM2 on the levels of tyrosine phosphorylation and bound to EGFR of GAREM2 dependent on EGF stimulation. a Schematics of the primary structure of FLAG-tagged full length GAREM2 (upper panel) and its deletion constructs lacking GRD (∆GRD186-209 and ∆GRD172-209). b Reduction of the tyrosine phosphorylation level of GAREM2 lacking GRD. All recombinant proteins were expressed as the N-terminal FLAG-tagged form. Each construct was transfected into COS-7 cells, and immunoprecipitation studies were carried out using the cell lysates from COS-7 cells. Each FLAG-tagged molecule was immunoprecipitated with an anti-FLAG antibody. FLAG-GAREM2 derivatives were visualized by CBB staining (bottom panel). Immunoblot analysis was carried out using an anti-pY20 antibody (middle panel) or an anti-EGFR antibody (upper panel). The levels of the tyrosine phosphorylation of FLAG-GAREM2 derivatives were quantified by densitometry. The representative results from three independent experiments are indicated below each panel. The amounts of FLAG-GAREM2 mutants are normalized to the control (wild type FLAG-GAREM2). c Graph showing the percentage of apoptosis induced by expressing each GFP-fused protein as indicated

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