G protein-coupled receptor kinases. Export

@article{citeulike:2871272, abstract = {G 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.}, address = {Howard Hughes Medical Institute, Department of Medicine (Cardiology), Duke University Medical Center, Durham, North Carolina 27710, USA. pitch001@mc.duke.edu}, author = {Pitcher, J. A. and Freedman, N. J. and Lefkowitz, R. J.}, citeulike-article-id = {2871272}, citeulike-linkout-0 = {http://dx.doi.org/10.1146/annurev.biochem.67.1.653}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/9759500}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=9759500}, doi = {10.1146/annurev.biochem.67.1.653}, issn = {0066-4154}, journal = {Annual review of biochemistry}, keywords = {gpcr, grk, lefkowitz, review}, pages = {653--692}, posted-at = {2008-06-07 15:04:24}, priority = {2}, title = {G protein-coupled receptor kinases.}, url = {http://dx.doi.org/10.1146/annurev.biochem.67.1.653}, volume = {67}, year = {1998} }

TY - JOUR ID - citeulike:2871272 L3 - citeulike-article-id:2871272 N2 - G 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. JF - Annual review of biochemistry SN - 0066-4154 AD - Howard Hughes Medical Institute, Department of Medicine (Cardiology), Duke University Medical Center, Durham, North Carolina 27710, USA. pitch001@mc.duke.edu EP - 692 TI - G protein-coupled receptor kinases. VL - 67 SP - 653 KW - gpcr KW - grk KW - lefkowitz KW - review AU - Pitcher, JA AU - Freedman, NJ AU - Lefkowitz, RJ PY - 1998/// UR - http://dx.doi.org/10.1146/annurev.biochem.67.1.653 ER -