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

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 chemo...

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Bibliographic Details
Published in:	Handbook of experimental pharmacology Vol. 219; p. 341
Main Authors:	McGovern, Kathryn W, DeFea, Kathryn A
Format:	Journal Article
Language:	English
Published:	Germany 2014
Subjects:	Actin Cytoskeleton - metabolism Actins - metabolism Animals Arrestins - metabolism beta-Arrestins Cell Movement - physiology Chemotaxis - physiology Humans Receptors, Chemokine - metabolism Receptors, G-Protein-Coupled - metabolism Signal Transduction - physiology
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Summary:	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.
ISSN:	0171-2004
DOI:	10.1007/978-3-642-41199-1_17