Identification of a trafficking determinant localized to the Kv1 potassium channel pore

Louis N. Manganas, Qiang Wang, Robert H. Scannevin, Dana E. Antonucci, Kenneth J. Rhodes, James Trimmer

Research output: Contribution to journalArticle

77 Scopus citations

Abstract

The repertoire of Kv1 potassium channels expressed in presynaptic terminals of mammalian central neurons is shaped by intrinsic trafficking signals that determine surface-expression efficiencies of homomeric and heteromeric Kv1 channel complexes. Here, we show that a determinant controlling surface expression of Kv1 channels is localized to the highly conserved pore region. Point-mutation analysis revealed two residues as critical for channel trafficking, one in the extracellular "turret" domain and one in the region distal to the selectivity filter. Interestingly, these same residues also form the binding sites for polypeptide neurotoxins. Our findings demonstrate a previously uncharacterized function for the channel-pore domain as a regulator of channel trafficking.

Original languageEnglish (US)
Pages (from-to)14055-14059
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume98
Issue number24
DOIs
StatePublished - Nov 20 2001
Externally publishedYes

ASJC Scopus subject areas

  • Genetics
  • General

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