Reference : The intracellular tyrosine residues of the ATP-gated P2X(1) ion channel are essential...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/23408
The intracellular tyrosine residues of the ATP-gated P2X(1) ion channel are essential for its function.
English
Oury, Cécile mailto [Université de Liège - ULg > Département des sciences biomédicales et précliniques > GIGA-R : Génétique humaine >]
Toth-Zsamboki, Emese [Katholieke Universiteit Leuven - KUL > Molecular and Cellular Medicine > CMVB > >]
Watanabe, Hiroyuki [Katholieke Universiteit Leuven - KUL > Molecular and Cellular Medicine > Laboratory of Physiology > >]
Nilius, Bernd [Katholieke Universiteit Leuven - KUL > Molecular and Cellular Medicine > Laboratory of Physiology > >]
Vermylen, Jos [Katholieke Universiteit Leuven - KUL > Molecular and Cellular Medicine > CMVB > >]
Hoylaerts, Marc F [Katholieke Universiteit Leuven - KUL > Molecular and Cellular Medicine > CMVB > >]
2002
FEBS Letters
Elsevier Science
Yes (verified by ORBi)
International
0014-5793
Amsterdam
The Netherlands
[en] purinergic receptors ; mutagenesis ; electrophysiology
[en] In this study, we mutated 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.
http://hdl.handle.net/2268/23408

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