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- W1995955688 abstract "It has been proposed that the pI(Cln) protein forms a nucleotide-sensitive plasma membrane anion channel with a GXGXG motif being an essential component of the extracellular nucleotide-binding site. To evaluate this hypothesis, we have performed voltage-clamp experiments on Xenopus laevis oocytes injected with RNA encoding a rat mutant pI(Cln) in which the three glycines of the putative nucleotide-binding site have been changed into alanines (G54A; G56A; G58A). The injected oocytes displayed outwardly rectifying anion currents, which were voltage-dependently blocked by extracellular cAMP, but which were not affected by removal of extracellular Ca2+. Furthermore, the mutation did not affect the voltage-dependent inactivation. We therefore conclude that there is no evidence in favour of an extracellular nucleotide-binding site in pI(Cln)." @default.
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- W1995955688 date "1998-04-17" @default.
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- W1995955688 title "The GXGXG motif in the pI<sub>Cln</sub> protein is not important for the nucleotide sensitivity of the pI<sub>Cln</sub> -induced Cl<sup>−</sup> current in <i>Xenopus</i> oocytes" @default.
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- W1995955688 doi "https://doi.org/10.1016/s0014-5793(98)00334-2" @default.
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