β-Arrestin-mediated PDE4 cAMP phosphodiesterase recruitment regulates β-adrenoceptor switching from Gs to Gi

Phosphorylation of the β 2 adrenoreceptor (β 2 AR) by cAMP-activated protein kinase A (PKA) switches its predominant coupling from stimulatory guanine nucleotide regulatory protein (G s ) to inhibitory guanine nucleotide regulatory protein (G i ). β-Arrestins recruit the cAMP-degrading PDE4 phosphod...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2003-02, Vol.100 (3), p.940-945
Hauptverfasser:	Baillie, George S, Sood, Arvind, McPhee, Ian, Gall, Irene, Perry, Stephen J, Lefkowitz, Robert J, Houslay, Miles D
Format:	Artikel
Sprache:	eng
Schlagworte:	3',5'-Cyclic-AMP Phosphodiesterases - metabolism Animals Animals, Newborn Arrestins - metabolism beta-Arrestins Biological Sciences Cell Line Cells, Cultured Cyclic AMP - metabolism Cyclic AMP-Dependent Protein Kinases - metabolism Cyclic Nucleotide Phosphodiesterases, Type 3 Cyclic Nucleotide Phosphodiesterases, Type 4 Enzyme Activation Enzyme Inhibitors - pharmacology Genes, Dominant Green Fluorescent Proteins Humans Isoquinolines - pharmacology Luminescent Proteins - metabolism Models, Biological Myocardium - cytology Neurology Neurotransmitters Pertussis Toxin - pharmacology Phosphoric Diester Hydrolases - metabolism Phosphorylation Rats Receptors, Adrenergic, beta - metabolism Rolipram - pharmacology Signal Transduction Sulfonamides Time Factors Transfection
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