Exchange of conductance and gating properties between gap junction hemichannels

Xinge Hu, Gerhard Dahl

Research output: Contribution to journalArticlepeer-review

33 Scopus citations


Gap junction channels span the membranes of two adjacent cells and allow the gated transit of molecules as large as second messengers from cell to cell. The structure of the gap junction channel pore is not resolved. For identification of pore determinants we used a chimera of two connexins, cx46 and cx32E143, that form membrane channels with distinct unit conductances and channel kinetics. Exchange of the first transmembrane segment (M1) between these connexins resulted in a chimera that exhibited most of the channel properties of the M1 donor, including single channel conductance, channel kinetics, and the preference to dwell at a subconductance level. The M1 segment thus appears to be an important determinant of conductance and gating properties of connexin channels. Copyright (C) 1999 Federation of European Biochemical Societies.

Original languageEnglish (US)
Pages (from-to)113-117
Number of pages5
JournalFEBS letters
Issue number2
StatePublished - May 21 1999


  • Channel
  • Chimera
  • Connexin
  • Gap junction
  • Patch clamp
  • Pore

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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