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This study investigates the role of AIP (AIP1) in modulating MAP kinase activation in Jurkat T cells. Following transfection with siGFP or siAIP1 and stimulation with P/I, we observed a significant reduction in phosphorylation of JNK (p54), while ERK phosphorylation remained unaffected. Western blotting analyses were conducted to assess the levels of JNK and ERK activation. Our findings suggest a selective impact of AIP on MAP kinase pathways, specifically highlighting its role in regulating JNK phosphorylation.
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siGFP siAIP1 0 12 20 40 0 12 20 40 P/I (min) pERK 1/2 35- ERK 1/2 35- Additional file 3Effects of AIP on MAP kinase activation. JNKp54 phosphorylation is diminished after AIP knockdown, while ERK phosphorylation is untouched. Jurkat T cells were transfected with siGFP or siAIP1 and stimulated with P/I as indicated. ERK and JNK phosphorylation was analyzed by western blotting. 55- pJNKp54 pJNKp46 40- 55- JNK 1/2 40- AIP 35- p65 65- Additional file3