Modulation of ion channel function by P2Y receptors.
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.
Lee
So Yeong
SY
Department of Physiology and the Molecular Veterinary Biosciences Graduate Program, University of Minnesota, Animal Science/Veterinary Medicine, St. Paul, MN 55108, USA.
O'Grady
Scott M
SM
D000818:Animals; D002462:Cell Membrane / Q000502:physiology*; D019204:GTP-Binding Proteins / Q000378:metabolism*; D006706:Homeostasis / Q000502:physiology*; D006801:Humans; D015640:Ion Channel Gating / Q000502:physiology*; D007473:Ion Channels / Q000502:physiology*; D008564:Membrane Potentials / Q000502:physiology*; D009865:Oocytes / Q000502:physiology; D017434:Protein Structure, Tertiary; D018048:Receptors, Purinergic P2 / Q000737:chemistry* / Q000502:physiology*; D013329:Structure-Activity Relationship; D014982:Xenopus laevis
D007473:Ion Channels; D018048:Receptors, Purinergic P2; D019204:GTP-Binding Proteins