Journal
CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 66, Issue 18, Pages 2953-2973Publisher
SPRINGER BASEL AG
DOI: 10.1007/s00018-009-0088-1
Keywords
G protein-coupled receptor; G protein; Arrestin; Desensitization; Endocytosis; Signal transduction
Categories
Funding
- National Institutes of Health [DK055524, HL007260]
- Department of Veterans Affairs Research Enhancement Award Program
- Ralph H. Johnson Veterans Affairs Medical Center
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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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