Modulation of ion channel function by P2Y receptors

Authors: Lee, So¹; O'Grady, Scott²

Source: Cell Biochemistry and Biophysics, Volume 39, Number 1, February 2003 , pp. 75-88(14)

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Abstract:

P2Y receptors are classified as P2 purinergic receptors that belong to the superfamily of G-protein coupled receptors. They are distinguishable from P1 (adenosine) receptors in that they bind adenine and/or uracil nucleotide triphosphates or diphosphates depending on the subtype. Over the past decade, P2Y receptors have been cloned from a variety of tissues and species. Eight functional subtypes have been characterized. Nucleotide binding produces activation of specific G-proteins that in turn regulate the function of membrane bound enzymes including phospholipase C and adenylyl cyclase. Certain P2Y receptor subtypes possess a PDZ domain located at the end of the C-terminal region of the receptor. PDZ domains have been established as sites for protein-protein interaction, thus providing a possible mechanism for receptor modulation of membrane protein function independent of G-protein activation. In this review we discuss recent findings that suggest that P2Y receptors can modulate the function of ion channels through multiple protein-protein interactions at the plasma membrane that do not directly involve G-protein activation.

Keywords: G-protein coupled receptor; sulfonylurea receptor; inwardly rectifying K+ channels; CFTR; PDZ domains

Document Type: Research article

DOI: http://dx.doi.org/10.1385/CBB:39:1:75

Affiliations: 1: Department of Physiology and the Molecular Veterinary Biosciences Graduate Program, University of Minnesota, Animal Science/Veterinary Medicine, 55108, St. Paul, MN, 2: Department of Physiology and the Molecular Veterinary Biosciences Graduate Program, University of Minnesota, Animal Science/Veterinary Medicine, 55108, St. Paul, MN, Email: ograd001@umn.edu

Publication date: 2003-02-01