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

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

Research output: Contribution to journalArticle

66 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 (US)
Pages (from-to)5-11
Number of pages7
JournalProceedings of the Royal Society B: Biological Sciences
Volume243
Issue number1306
DOIs
StatePublished - Jan 1 1991

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)
  • Environmental Science(all)
  • Agricultural and Biological Sciences(all)

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