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.
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