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      Emerging paradigms of β-arrestin-dependent seven transmembrane receptor signaling.

      Trends in Biochemical Sciences

      Angiotensin II, analogs & derivatives, metabolism, Animals, Arrestins, Endocytosis, Extracellular Signal-Regulated MAP Kinases, Humans, Membrane Proteins, Phosphoproteins, Phosphorylation, Protein Conformation, Protein Transport, Receptors, G-Protein-Coupled, Signal Transduction, Species Specificity, Ubiquitination

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          Abstract

          β-Arrestins, originally discovered to desensitize activated seven transmembrane receptors (7TMRs; also known as G-protein-coupled receptors, GPCRs), are now well established mediators of receptor endocytosis, ubiquitylation and G protein-independent signaling. Recent global analyses of β-arrestin interactions and β-arrestin-dependent phosphorylation events have uncovered several previously unanticipated roles of β-arrestins in a range of cellular signaling events. These findings strongly suggest that the functional roles of β-arrestins are much broader than currently understood. Biophysical studies aimed at understanding multiple active conformations of the 7TMRs and the β-arrestins have begun to unravel the mechanistic basis for the diverse functional capabilities of β-arrestins in cellular signaling. Copyright © 2011 Elsevier Ltd. All rights reserved.

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          Author and article information

          Journal
          21764321
          3168679
          10.1016/j.tibs.2011.06.003

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