β-arrestin-mediated receptor trafficking and signal transduction

By Sudha K. Shenoy, R. J. Lefkowitz. TIPS - Trends in Pharmacological Sciences, 2011

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β-arrestins function as endocytic adaptors and mediate trafficking of a variety of cell-surface receptors, including seven-transmembrane receptors (7TMRs). In the case of 7TMRs, β-arrestins carry out these tasks while simultaneously inhibiting upstream G protein-dependent signaling and promoting alternate downstream signaling pathways. The mechanisms by which β-arrestins interact with a continuously expanding ensemble of protein partners and perform their multiple functions including trafficking and signaling are currently being uncovered. Molecular changes at the level of protein conformation as well as posttranslational modifications of β-arrestins likely form the basis for their dynamic interactions during receptor trafficking and signaling. It is becoming increasingly evident that β-arrestins, originally discovered as 7TMR adaptor proteins, indeed have much broader and more versatile roles in maintaining cellular homeostasis. Here we review the traditional and novel functions of β-arrestins and discuss the molecular attributes that might facilitate it multiple interactions in regulating cell signaling and receptor trafficking.

Subfields: Cellular and Molecular Neuroscience, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/55dfd39d4a563863fec2be717e6027cc023f80c9