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Contribution of P2X1 receptor intracellular basic residues to channel properties

By Catherine Vial, Richard Rigby and Richard J. Evans

Abstract

This paper was published as Biochemical and Biophysical Research Communications, 2006, 350 (1), pp. 244-248. It is available from http://www.sciencedirect.com/science/journal/0006291X. Doi: 10.1016/j.bbrc.2006.09.038Metadata only entryThe intracellular amino and carboxy termini of P2X receptors have been shown to contribute to the regulation of ATP evoked currents. In this study we produced, and expressed in Xenopus oocytes, individual alanine point mutants of positively charged amino acids (eight lysine, seven arginine and one histidine) in the intracellular domains of the human P2X1 receptor. The majority of these mutations had no effect on the amplitude, time-course or rectification of ATP evoked currents. In contrast the mutant K367A was expressed at normal levels at the cell surface however ATP evoked currents were reduced by >99% and desensitised more rapidly demonstrating a role of K367 in channel regulation. This is similar to that previously described for T18A mutant channels. Co-expression of T18A and K367A mutant P2X1 receptors produced larger ATP evoked responses than either mutant alone and suggests that these amino and carboxy terminal regions interact to regulate channel function

Publisher: Elsevier
Year: 2006
DOI identifier: 10.1016/j.bbrc.2006.09.038
OAI identifier: oai:lra.le.ac.uk:2381/8046
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