title: Molecular mechanisms underlying beta-arrestin-dependent chemotaxis and actin-cytoskeletal reorganization.
abstract: 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.
authors.affiliation: Biochemistry and Molecular Biology Graduate Program, University of California, Riverside, CA, USA.
authors.forename: Kathryn W
authors.initials: KW
authors.lastname: McGovern
authors.forename: Kathryn A
authors.initials: KA
authors.lastname: DeFea
mesh_terms: D008841:Actin Cytoskeleton / Q000378:metabolism*; D000199:Actins / Q000378:metabolism; D000818:Animals; D019390:Arrestins / Q000378:metabolism*; D002465:Cell Movement / Q000502:physiology; D002633:Chemotaxis / Q000502:physiology*; D006801:Humans; D019707:Receptors, Chemokine / Q000378:metabolism; D043562:Receptors, G-Protein-Coupled / Q000378:metabolism; D015398:Signal Transduction / Q000502:physiology; D000071557:beta-Arrestins
chemical_list: D000199:Actins; D019390:Arrestins; D019707:Receptors, Chemokine; D043562:Receptors, G-Protein-Coupled; D000071557:beta-Arrestins