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pubmed-article:9759500pubmed:abstractTextG protein-coupled receptor kinases (GRKs) constitute a family of six mammalian serine/threonine protein kinases that phosphorylate agonist-bound, or activated, G protein-coupled receptors (GPCRs) as their primary substrates. GRK-mediated receptor phosphorylation rapidly initiates profound impairment of receptor signaling, or desensitization. This review focuses on the regulation of GRK activity by a variety of allosteric and other factors: agonist-stimulated GPCRs, beta gamma subunits of heterotrimeric GTP-binding proteins, phospholipid cofactors, the calcium-binding proteins calmodulin and recoverin, posttranslational isoprenylation and palmitoylation, autophosphorylation, and protein kinase C-mediated GRK phosphorylation. Studies employing recombinant, purified proteins, cell culture, and transgenic animal models attest to the general importance of GRKs in regulating a vast array of GPCRs both in vitro and in vivo.lld:pubmed
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pubmed-article:9759500pubmed:authorpubmed-author:PitcherJ AJAlld:pubmed
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pubmed-article:9759500pubmed:dateRevised2007-11-15lld:pubmed
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pubmed-article:9759500pubmed:year1998lld:pubmed
pubmed-article:9759500pubmed:articleTitleG protein-coupled receptor kinases.lld:pubmed
pubmed-article:9759500pubmed:affiliationHoward Hughes Medical Institute, Department of Medicine (Cardiology), Duke University Medical Center, Durham, North Carolina 27710, USA. pitch001@mc.duke.edulld:pubmed
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