FEBS Letters | |
The GXGXG motif in the pICln protein is not important for the nucleotide sensitivity of the pICln‐induced Cl− current in Xenopus oocytes | |
Eggermont, Jan1  Voets, Thomas1  Nilius, Bernd1  Buyse, Gunnar1  Droogmans, Guy1  | |
[1] Katholieke Universiteit Leuven, Laboratorium voor Fysiologie Campus Gasthuisberg O and N, B-3000 Leuven, Belgium | |
关键词: Anion channel; Oocyte; Cyclic adenosine monophosphate; | |
DOI : 10.1016/S0014-5793(98)00334-2 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
It has been proposed that the pICln 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 pICln 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 pICln.
【 授权许可】
Unknown
【 预 览 】
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