Differential interaction of voltage-gated K+ channel β-subunits with cytoskeleton is mediated by unique amino terminal domains

Kensuke Nakahira, Maria F. Matos, James Trimmer

Research output: Contribution to journalArticle

22 Scopus citations

Abstract

To define the molecular characteristics of K+ channel β-subunit polypeptides, we have studied their biochemical properties and subcellular distribution in transfected mammalian cells. We find that the recombinant voltage-dependent K+ (Kv) β1.1 and Kvβ2 polypeptides have distinct detergent solubility properties owing to a novel association of Kvβ1.1 with the actin-based cytoskeleton. Mutational and chimeric protein analyses show that the unique amino-terminus of Kvβ1.1 is both necessary and sufficient for mediating the association of β-subunits with cytoskeleton. Thus, the interaction with cytoskeleton is mediated through the amino-terminal domain previously shown to be necessary for modulating α-subunit inactivation, but not necessary for interaction with α-subunit polypeptides. These data reveal that different domains of β-subunit polypeptides mediate interactions with cytoskeleton and with α-subunits, and provide a structural basis for previous reports that linked the extent of β-subunit-induced inactivation to the state of the actin cytoskeleton.

Original languageEnglish (US)
Pages (from-to)199-208
Number of pages10
JournalJournal of Molecular Neuroscience
Volume11
Issue number3
DOIs
StatePublished - 1998
Externally publishedYes

Keywords

  • Central nervous system
  • Epilepsy
  • Excitability
  • Ion channel
  • Localization
  • Modulation

ASJC Scopus subject areas

  • Neuroscience(all)
  • Biochemistry
  • Genetics

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