This item still needs to be validated !
Title: The intracellular tyrosine residues of the ATP-gated P2X(1) ion channel are essential for its function
Authors: Toth-Zsamboki, Emese
Oury, Cecile
Watanabe, Hiroyuki
Nilius, Bernd
Vermylen, Jos
Hoylaerts, Marc # ×
Issue Date: Jul-2002
Series Title: FEBS Letters vol:524 issue:1-3 pages:15-9
Abstract: The four highly conserved intracellular tyrosine residues of the P2X(1) ion channel were mutated into phenylalanine. Simultaneous electrophysiological and calcium measurements in transfected human embryonic kidney (HEK 293) cells indicated that Y362F and Y370F mutants were non-functional, despite their proper plasma membrane expression. The Y16F and Y363F mutants retained 2.2% and 26% of the wild-type P2X(1) activity, respectively. However, no tyrosine phosphorylation was detected on Western blots of P2X(1) immunoprecipitates derived either from HEK 293 cell lysates or from human platelets, expressing P2X(1) endogenously. Thus, Y16, Y362, Y363 and Y370 are required for the appropriate three-dimensional structure and function of the intracellular P2X(1) domains.
ISSN: 0014-5793
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Physiology Section (-)
Molecular and Vascular Biology
Laboratory of Ion Channel Research (VIB-KU Leuven Center for Brain & Disease Research)
Department of Cellular and Molecular Medicine - miscellaneous
× 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