Molecular mechanisms underlying beta-arrestin-dependent chemotaxis and actin-cytoskeletal reorganization.

ß-Arrestins play a crucial role in cell migration downstream of multiple G-protein-coupled receptors (GPCRs) through multiple mechanisms. There is considerable evidence that ß-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 ß-arrestins facilitate receptor turnover through their ability to desensitize and internalize GPCRs. This chapter discusses both theories for ß-arrestin-dependent chemotaxis in the context of recent studies, specifically addressing known actin assembly proteins regulated by ß-arrestins, chemokine receptors, and signaling by chemotactic receptors.