β-Arrestins play a crucial role in cell migration downstream of multiple G-protein-coupled receptors (GPCRs) through multiple mechanisms. There is considerable evidence that β-arrestin-dependent scaffolding of actin assembly proteins facilitates the formation of a leading edge in response to a chemotactic signal. Conversely, there is substantial support for the hypothesis that β-arrestins facilitate receptor turnover through their ability to desensitize and internalize GPCRs. This chapter discusses both theories for β-arrestin-dependent chemotaxis in the context of recent studies, specifically addressing known actin assembly proteins regulated by β-arrestins, chemokine receptors, and signaling by chemotactic receptors. © 2014 Springer-Verlag Berlin Heidelberg.
CITATION STYLE
McGovern, K. W., & Defea, K. A. (2014). Molecular mechanisms underlying beta-arrestin-dependent chemotaxis and actin-cytoskeletal reorganization. Handbook of Experimental Pharmacology, 219, 341–359. https://doi.org/10.1007/978-3-642-41199-1_17
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