Modulation of ion channel function by P2Y receptors

Yeong Lee So, Scott M. O'Grady

Research output: Contribution to journalReview articlepeer-review

8 Scopus citations

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 languageEnglish (US)
Pages (from-to)75-88
Number of pages14
JournalCell biochemistry and biophysics
Volume39
Issue number1
DOIs
StatePublished - Aug 1 2003

Keywords

  • CFTR
  • G-protein coupled receptor
  • Inwardly rectifying K+ channels
  • PDZ domains
  • Sulfonylurea receptor

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