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lüll The role of beta-arrestins in the termination and transduction of G-protein-coupled receptor signals Luttrell LM; Lefkowitz RJJ Cell Sci 2002[Feb]; 115 (Pt 3): 455-65beta-Arrestins are versatile adapter proteins that form complexes with most G-protein-coupled receptors (GPCRs) following agonist binding and phosphorylation of receptors by G-protein-coupled receptor kinases (GRKs). They play a central role in the interrelated processes of homologous desensitization and GPCR sequestration, which lead to the termination of G protein activation. beta-arrestin binding to GPCRs both uncouples receptors from heterotrimeric G proteins and targets them to clathrin-coated pits for endocytosis. Recent data suggest that beta-arrestins also function as GPCR signal transducers. They can form complexes with several signaling proteins, including Src family tyrosine kinases and components of the ERK1/2 and JNK3 MAP kinase cascades. By recruiting these kinases to agonist-occupied GPCRs, beta-arrestins confer distinct signaling activities upon the receptor. beta-arrestin-Src complexes have been proposed to modulate GPCR endocytosis, to trigger ERK1/2 activation and to mediate neutrophil degranulation. By acting as scaffolds for the ERK1/2 and JNK3 cascades, beta-arrestins both facilitate GPCR-stimulated MAP kinase activation and target active MAP kinases to specific locations within the cell. Thus, their binding to GPCRs might initiate a second wave of signaling and represent a novel mechanism of GPCR signal transduction.|Animals[MESH]|Arrestins/genetics/*metabolism[MESH]|Biological Transport/physiology[MESH]|Down-Regulation[MESH]|GTP-Binding Proteins/*metabolism[MESH]|Mitogen-Activated Protein Kinases/metabolism[MESH]|Models, Biological[MESH]|Receptors, Cell Surface/*metabolism[MESH]|Signal Transduction/*physiology[MESH]|beta-Arrestins[MESH]|src-Family Kinases/metabolism[MESH] |