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ADRBK1 (GRK2) is a serine/threonine kinase. Many of the G protein-coupled receptors are known to be phosphorylated by G protein-dependent receptor kinases (GRKs). G protein-coupled receptor kinases (GRKs) are important regulators of G protein-coupled receptors(GPCRs). GRK2 (83 kDa), one of six members of this family that have been identified, is ubiquitously expressed in mammals. After binding to their ligand and interacting with heterotrimeric G proteins, GPCRs (e.g., a2-adrenergic receptor) are phosphorylated by GRKs. Internalization of the GPCRs, regulated by beta-arrestin-1, leads to activation of the Ras - Raf - ERK1&2 signaling pathway. GRK2 activity is tightly controlled by different mechanisms including phosphorylation by kinases such as PKC, Src and ERK1&2, as well as interaction with various proteins. ERK phosphorylates and thus inactivates GRK2 on serine 670 in a negative feedback mechanism.
ADRBK1; Adrbk-1; adrenergic beta receptor kinase 1; adrenergic receptor kinase, beta 1; adrenergic, beta, receptor kinase 1; BARK; BARK1; Bark-1; beta ARK; Beta-adrenergic receptor kinase 1; beta-adrenergic receptor kinase 1 beta ARK1; beta-AR kinase-1; betaARK1; BETA-ARK1; beta-ARK-1; EC 2.7.1.126; G protein-coupled receptor kinase 2; G-protein coupled receptor kinase 2; G-protein-coupled receptor kinase 2; grk 2; Grk2; GRK-2
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