Contributions of the C-terminal domain to gating properties of inward rectifier potassium channels

M. Pessia, C. T. Bond, M. P. Kavanaugh, J. P. Adelman

Research output: Contribution to journalArticle

34 Scopus citations

Abstract

Two inward rectifier potassium channels, the G protein-dependent GIRK1 and the G protein-independent BIR10, display large differences in rectification and macroscopic kinetics. A chimeric channel was constructed in which the putative intracellular carboxy-terminal domain of the G protein-dependent channel replaced the corresponding domain of the G protein-independent channel. The chimeric channel conducted potassium ions without the requirement of activated G proteins, yet displayed activation and deactivation kinetics and rectification properties similar to those of the G protein-dependent channel. The results demonstrate that structural elements in the C-terminus can independently control gating but not G protein signal transduction. The voltage dependence, time course, and kinetics of gating suggest a mechanism in which the pore may be occluded by reversible interactions with charged residues in the C-terminus.

Original languageEnglish (US)
Pages (from-to)1039-1045
Number of pages7
JournalNeuron
Volume14
Issue number5
DOIs
StatePublished - May 1995

ASJC Scopus subject areas

  • Neuroscience(all)

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