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The intracellular tyrosine residues of the ATP-gated P2X1 ion channel are essential for its function
- Source :
- FEBS Letters. (1-3):15-19
- Publisher :
- Federation of European Biochemical Societies. Published by Elsevier B.V.
-
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.
- Subjects :
- Molecular Sequence Data
Biophysics
Phenylalanine
Biology
ATP-gated non-selective cation channel
Biochemistry
Cell Line
chemistry.chemical_compound
Adenosine Triphosphate
Tyrosine residue
Structural Biology
Genetics
Humans
Amino Acid Sequence
Tyrosine
Phosphorylation
Molecular Biology
Ion channel
DNA Primers
Site-directed mutagenesis
Base Sequence
Sequence Homology, Amino Acid
Receptors, Purinergic P2
HEK 293 cells
Tyrosine phosphorylation
Cell Biology
Three-dimensional structure
chemistry
P2X1 receptor
Receptors, Purinergic P2X
Mutagenesis, Site-Directed
Adenosine triphosphate
Ion Channel Gating
Intracellular
Subjects
Details
- Language :
- English
- ISSN :
- 00145793
- Issue :
- 1-3
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....f8fbd7a18ea463b508ac47f682291c7e
- Full Text :
- https://doi.org/10.1016/S0014-5793(02)02987-3