Identification and characterization of novel components of a Ca 2+/calmodulin-dependent protein kinase cascade in HeLa cells

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Abstract

In this report, we cloned a novel calmodulin-kinase (CaM-KIδ) from HeLa cells and characterized its activation mechanism. CaM-KIδ exhibits Ca2+/CaM-dependent activity that is enhanced (∼30-fold) in vitro by phosphorylation of its Thr180 by CaM-K kinase (CaM-KK)α, consistent with detection of CaM-KIδ-activating activity in HeLa cells. We also identified a novel CaM-KKβ isoform (CaM-KKβ-3) in HeLa cells whose activity was highly Ca2+/CaM-independent. Transiently expressed CaM-KIδ exhibited enhanced protein kinase activity in HeLa cells without ionomycin stimulation. This sustained activation of CaM-KIδ was completely abolished by Thr180Ala mutation and inhibited by CaM-KK inhibitor, STO-609, indicating a functional CaM-KK/CaM-KIδ cascade in HeLa cells. © 2003 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.

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Ishikawa, Y., Tokumitsu, H., Inuzuka, H., Murata-Hori, M., Hosoya, H., & Kobayashi, R. (2003). Identification and characterization of novel components of a Ca 2+/calmodulin-dependent protein kinase cascade in HeLa cells. FEBS Letters, 550(1–3), 57–63. https://doi.org/10.1016/S0014-5793(03)00817-2

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