Diversity in arrestin function |
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Authors: | Ryan T Kendall Louis M Luttrell |
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Institution: | (1) Department of Medicine, Medical University of South Carolina, Charleston, SC 29425, USA;(2) Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC 29425, USA;(3) Ralph H. Johnson Veterans Affairs Medical Center, Charleston, SC 29401, USA;(4) Division of Endocrinology, Diabetes and Medical Genetics, Medical University of South Carolina, 96 Jonathan Lucas Street, Suite 816 CSB, MSC 624, Charleston, SC 29425, USA; |
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Abstract: | The termination of heptahelical receptor signaling is a multilevel process coordinated, in large part, by members of the arrestin
family of proteins. Arrestin binding to agonist-occupied receptors promotes desensitization by interrupting receptor-G protein
coupling, while simultaneously recruiting machinery for receptor endocytosis, vesicular trafficking, and receptor fate determination.
By simultaneously binding other proteins, arrestins also act as ligand-regulated scaffolds that recruit protein and lipid
kinase, phosphatase, phosphodiesterase, and ubiquitin ligase activity into receptor-based multiprotein ‘signalsome’ complexes.
Arrestin-binding thus ‘switches’ receptors from a transient G protein-coupled state to a persistent arrestin-coupled state
that continues to signal as the receptor transits intracellular compartments. While it is clear that signalsome assembly has
profound effects on the duration and spatial characteristics of heptahelical receptor signals, the physiologic functions of
this novel signaling mechanism are poorly understood. Growing evidence suggests that signalsomes regulate such diverse processes
as endocytosis and exocytosis, cell migration, survival, and contractility. |
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