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Title: A natural dominant negative P2X1 receptor due to deletion of a single amino acid residue
Authors: Oury, C├ęcile
Toth-Zsamboki, E
Van Geet, Christel
Thys, C
Wei, L
Nilius, Bernd
Vermylen, Jozef
Hoylaerts, Marc # ×
Issue Date: Aug-2000
Series Title: Journal of Biological Chemistry vol:275 issue:30 pages:22611-4
Abstract: The P2X1 receptor belongs to a family of oligomeric ATP-gated ion channels with intracellular N and C termini and two transmembrane segments separating a large extracellular domain. Here, we describe a naturally occurring dominant negative P2X1 mutant. This mutant lacks one leucine within a stretch of four leucine residues in its second transmembrane domain (TM2) (amino acids 351-354). Confocal microscopy revealed proper plasma membrane localization of the mutant in stably transfected HEK293 cells. Nevertheless, voltage-clamped HEK293 cells expressing mutated P2X1 channels failed to develop an ATP or ADP-induced current. Furthermore, when co-expressed with the wild type receptor in Xenopus oocytes, the mutated protein exhibited a dose-dependent dominant negative effect on the normal ATP or ADP-induced P2X1 channel activity. These data indicate that deletion of a single apolar amino acid residue at the inner border of the P2X1 TM2 generates a nonfunctional channel. The inactive and dominant negative form of the P2X1 receptor may constitute a new tool for the study of the physiological role of this channel in native cells.
URI: 
ISSN: 0021-9258
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Molecular and Vascular Biology
Laboratory of Ion Channel Research
Department of Cellular and Molecular Medicine - miscellaneous
Faculty of Medicine - miscellaneous
× corresponding author
# (joint) last author

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