CAMK1δ or Ca2+/calmodulin-dependent kinase I-like kinase (CKLiK) is activated by Ca2+ and calmodulin and is detected in CD34+-derived neutrophils and eosinophils, as well as in mature peripheral blood granulocytes.CAMK1δ exhibits Ca2+/CaM-dependent activity that is enhanced in vitro by phosphorylation of its Thr180 by CaM-K kinase (CaM-KK)alpha, consistent with detection of CAMK1δ-activating activity in HeLa cells.
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Activation of granulocyte effector functions, such as induction of the respiratory burst and migration, are regulated by a variety of relatively ill-defined signaling pathways. Recently, we identified a novel Ca2+/calmodulin-dependent kinase I-like kinase, CKLiK, which exhibits restricted mRNA expression to
In this report, we cloned a novel calmodulin-kinase (CaM-KIdelta) from HeLa cells and characterized its activation mechanism. CaM-KIdelta exhibits Ca(2+)/CaM-dependent activity that is enhanced (approximately 30-fold) in vitro by phosphorylation of its Thr180 by CaM-K kinase (CaM-KK)alpha, consistent with detection
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