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 |
|---|---|
| Pages (from-to) | 5-11 |
| Number of pages | 7 |
| Journal | Proceedings of the Royal Society B: Biological Sciences |
| Volume | 243 |
| Issue number | 1306 |
| State | Published - Feb 13 1991 |
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ASJC Scopus subject areas
- Agricultural and Biological Sciences(all)
- Agricultural and Biological Sciences (miscellaneous)
Cite this
Gating properties of connexin32 cell-cell channels and their mutants expressed in Xenopus oocytes. / Werner, R.; Levine, E.; Rabadan-Diehl, C.; Dahl, Gerhard.
In: Proceedings of the Royal Society B: Biological Sciences, Vol. 243, No. 1306, 13.02.1991, p. 5-11.Research output: Contribution to journal › Article
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TY - JOUR
T1 - Gating properties of connexin32 cell-cell channels and their mutants expressed in Xenopus oocytes
AU - Werner, R.
AU - Levine, E.
AU - Rabadan-Diehl, C.
AU - Dahl, Gerhard
PY - 1991/2/13
Y1 - 1991/2/13
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=0026071778&partnerID=8YFLogxK
M3 - Article
C2 - 1673244
AN - SCOPUS:0026071778
VL - 243
SP - 5
EP - 11
JO - Proceedings of the Royal Society B: Biological Sciences
JF - Proceedings of the Royal Society B: Biological Sciences
SN - 0800-4622
IS - 1306
ER -