Identification of a proline residue as a transduction element involved in voltage gating of gap junctions

Thomas M. Suchyna, Lie Xian Xu, Feng Gao, Charles R. Fourtner, Bruce J. Nicholson

Research output: Contribution to journalArticle

130 Scopus citations

Abstract

GAP junction channels are structurally distinct from other ion channels in that they comprise two hemichannels which interact head-to-head to form an aqueous channel between cells. Intercellular voltage differences together with increased intracellular concentrations of H+ and Ca2+ cause closure of these normally patent channels1. The relative sensitivity to voltage varies with the subunit (connexin) composition of the channels2. The third of four transmembrane-spanning regions (M3) in connexins has been proposed to form the channel lining3, and a global 'tilting' of the hemichannel subunits has been correlated with channel closure4. But specific components involved in transduction of channel gating events have not been identified in either gap junctions or other ion channel classes (however, see model in ref. 5). We have examined a strictly conserved proline centrally located in M2 of connexin proteins. Mutation of this proline (Pro 87) in connexin 26 causes a reversal in the voltage-gating response when the mutant hemichannel is paired with wild-type connexin 26 in the Xenopus oocyte system. This suggests that the unique properties associated with this residue are critical to the transduction of voltage gating in these channels.

Original languageEnglish (US)
Pages (from-to)847-849
Number of pages3
JournalNature
Volume365
Issue number6449
DOIs
StatePublished - Jan 1 1993
Externally publishedYes

ASJC Scopus subject areas

  • General

Fingerprint Dive into the research topics of 'Identification of a proline residue as a transduction element involved in voltage gating of gap junctions'. Together they form a unique fingerprint.

  • Cite this

    Suchyna, T. M., Xu, L. X., Gao, F., Fourtner, C. R., & Nicholson, B. J. (1993). Identification of a proline residue as a transduction element involved in voltage gating of gap junctions. Nature, 365(6449), 847-849. https://doi.org/10.1038/365847a0