Journal
MOLECULAR AND CELLULAR BIOLOGY
Volume 26, Issue 14, Pages 5497-5508Publisher
TAYLOR & FRANCIS INC
DOI: 10.1128/MCB.02469-05
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CARMAI is a central regulator of NF-kappa B activation in lymphocytes. CARMA1 and BcI10 functionally interact and control NF-kappa B signaling downstream of the T-cell receptor (TCR). Computational analysis of expression neighborhoods of CARMA1-Bcl10MALT 1 for enrichment in kinases identified calmodulin-dependent protein kinase II (CaMKII) as an important component of this pathway. Here e report that Ca2+/CaMKHII redistributed to the immune synapse following T-cell activation and that CaMKHII is critical for NF-kappa B activation induced by TCR stimulation. Furthermore. CaMKII enhances GARMA1-induced NF-kappa B activation. Moreover, we have shown that CaMKII phosphorylates CARMA1 on Ser109 and that the phosphorylation facilitates the interaction between CARMAI and Bcl10. These results provide a novel function for CaMKII in TCR signaling and CARMAI-induced NF-kappa B activation.
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