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.
Original language | English (US) |
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Pages (from-to) | 75-88 |
Number of pages | 14 |
Journal | Cell biochemistry and biophysics |
Volume | 39 |
Issue number | 1 |
DOIs | |
State | Published - Aug 2003 |
Keywords
- CFTR
- G-protein coupled receptor
- Inwardly rectifying K+ channels
- PDZ domains
- Sulfonylurea receptor