Cloned Ca2+-dependent K+ channel modulated by a functionally associated protein kinase

Manuel Esguerra, Jing Wang, Christine D. Foster, John P. Adelman, R. Alan North, Irwin B. Levitan

Research output: Contribution to journalArticlepeer-review

98 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)563-565
Number of pages3
Issue number6481
StatePublished - 1994

ASJC Scopus subject areas

  • General


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