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.
journal_name
Cell Biochem Biophysjournal_title
Cell biochemistry and biophysicsauthors
Lee SY,O'Grady SMdoi
10.1385/CBB:39:1:75subject
Has Abstractpub_date
2003-01-01 00:00:00pages
75-88issue
1eissn
1085-9195issn
1559-0283pii
CBB:39:1:75journal_volume
39pub_type
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