Title: The GXGXG motif in the pI(Cln) protein is not important for the nucleotide sensitivity of the pI(Cln)-induced Cl- current in Xenopus oocytes
Authors: Voets, Thomas ×
Buyse, Gunnar
Droogmans, Guillaume
Eggermont, Jan
Nilius, Bernd #
Issue Date: Jun-1998
Series Title: FEBS Letters vol:426 issue:2 pages:171-3
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).
ISSN: 0014-5793
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Physiology Section (-)
Laboratory of Ion Channel Research (VIB-KU Leuven Center for Brain & Disease Research)
Brain & Metabolism Section (-)
Department of Cellular and Molecular Medicine - miscellaneous
Laboratory of Cellular Transport Systems
× corresponding author
# (joint) last author

Files in This Item:

There are no files associated with this item.

Request a copy


All items in Lirias are protected by copyright, with all rights reserved.

© Web of science