Gating properties of connexin32 cell-cell channels and their mutants expressed in Xenopus oocytes

R. Werner, E. Levine, C. Rabadan-Diehl, Gerhard Dahl

Research output: Contribution to journalArticle

65 Scopus citations

Abstract

Carboxyl-terminal deletion mutants of the gap junction protein connexin32 were tested in the oocyte cell-cell channel assay. Oocytes expressing a mutant lacking 58 carboxyl terminal amino acids were found to exhibit junctional conductances of the same magnitude as oocytes expressing wild-type connexin32. The gating properties of the channels formed by this mutant of connexin32 with respect to transjunctional voltage and cytoplasmic acidification are indistinguishable from those found with wild-type connexin32 channels. This includes a novel pH-dependent voltage gate. In another mutant, two carboxyl terminal serine residues, Ser233 and Ser240, were replaced by Asn residues. This double mutant has properties indistinguishable from wild-type connexin32, suggesting that phosphorylation of either of these serines is not required for channel opening.

Original languageEnglish
Pages (from-to)5-11
Number of pages7
JournalProceedings of the Royal Society B: Biological Sciences
Volume243
Issue number1306
StatePublished - Feb 13 1991

    Fingerprint

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Agricultural and Biological Sciences (miscellaneous)

Cite this