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 language | English (US) |
|---|---|
| Pages (from-to) | 5-11 |
| Number of pages | 7 |
| Journal | Proceedings of the Royal Society B: Biological Sciences |
| Volume | 243 |
| Issue number | 1306 |
| DOIs | |
| State | Published - 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)