Calnexin regulates mammalian Kv1 channel trafficking

Louis N. Manganas, James Trimmer

Research output: Contribution to journalArticlepeer-review

20 Scopus citations


Voltage-gated Kv1 channels are key factors regulating excitability in the mammalian central nervous system. Diverse posttranslational regulatory mechanisms operate to determine the density, subunit composition, and localization of Kv1 channel complexes in the neuronal plasma membrane. In this study, we investigated the role of the endoplasmic reticulum chaperone calnexin in the intracellular trafficking of Kv1 channels. We found that coexpressing calnexin with the Kv1.2α subunit in transfected mammalian COS-1 cells produced a dramatic dose-dependent increase in cell surface Kv1.2 channel complexes. In calnexin-transfected COS-1 cells, the proportion of Kv1.2 channels with mature N-linked oligosaccharide chains was comparable to that observed in neurons. In contrast, calnexin coexpression exerted no effects on trafficking of the intracellularly retained Kv1.1 or Kv1.6α subunits. We also found that calnexin and auxiliary Kvβ2 subunit coexpression was epistatic, suggesting that they share a common pathway for promoting Kv1.2 channel surface expression. These results provide yet another component in the elaborate repertoire of determinants regulating the density of Kv1 channels in the plasma membrane.

Original languageEnglish (US)
Pages (from-to)577-584
Number of pages8
JournalBiochemical and Biophysical Research Communications
Issue number2
StatePublished - Sep 17 2004


  • Biosynthesis
  • Endoplasmic reticulum
  • Ion channel
  • Membrane protein

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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