Abstract
CALCIUM-DEPENDENT potassium (Kca) channels carry ionic currents that regulate important cellular functions1–3. Like some other ion channels4–10, Kca channels are modulated by protein phosphorylation2,11,15–21. The recent cloning of complementary DNAs encoding Slo Kca channels12–14 has enabled Kca channel modulation to be investigated. We report here that protein phosphorylation modulates the activity of Drosophila Slo KCa channels expressed in Xenopus oocytes. Application of ATP-γS to detached membrane patches increases Slo channel activity by shifting channel voltage sensitivity. This modulation is blocked by a specific inhibitor of cyclic AMP-dependent protein kinase (PKA). Mutation of a single serine residue in the channel protein also blocks modulation by ATP-γS, demonstrating that phosphorylation of the Slo channel protein itself modulates channel activity. The results also indicate that Kca channels in oocyte membrane patches can be modulated by an endogenous PKA-like protein kinase which remains functionally associated with the channels in the detached patch.
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Esguerra, M., Wang, J., Foster, C. et al. Cloned Ca2+-dependent K+ channel modulated by a functionally associated protein kinase. Nature 369, 563–565 (1994). https://doi.org/10.1038/369563a0
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DOI: https://doi.org/10.1038/369563a0
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