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. 2007 Dec 3;179(5):923–934. doi: 10.1083/jcb.200708200

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Copyright © 2007, The Rockefeller University Press

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Figure 7. — Effect of IP₃R1 Y353 phosphorylation on NFAT activity. (A) Immunoblotting of lysates from 10⁶ transfected Jurkat T cells with anti-IP3R1 antibody showed comparable overexpression of WT-IP3R1 and IP3R1-Y353F. (B) Relative NFAT-dependent luciferase activity. 10⁶ Jurkat cells were transiently transfected with WT-IP₃R1, IP₃R1-Y353F, or pcDNA3.1 vector together with an NFAT–firefly luciferase reporter assay construct and a TK-Renilla luciferase construct as a control for luciferase transfection efficiency. After stimulation with OKT3 (anti-CD3 antibody), cells were lysed and the lysates were assayed for NFAT-luciferase activity, quenched, and assayed for TK-luciferase activity in triplicate. NFAT activity is expressed as relative NFAT luminescence normalized to TK luminescence and adjusted for IP₃R1 expression levels. The results are shown as fold stimulation over nonstimulated vector control. Data were presented as the mean ± SEM of seven independent Jurkat preparations assayed in triplicate. (*, P < 0.05 WT vs. vector by t test; **, P < 0.05 WT vs. Y353F by t test).