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Gating Properties of Connexin32 Cell--Cell Channels and their Mutants Expressed in Xenopus Oocytes
R. Werner, E. Levine, C. Rabadan-Diehl and G. Dahl
Proceedings: Biological Sciences
Vol. 243, No. 1306 (Jan. 22, 1991), pp. 5-11
Published by: Royal Society
Stable URL: http://www.jstor.org/stable/76508
Page Count: 7
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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.
Proceedings: Biological Sciences © 1991 Royal Society