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Handb Exp Pharmacol. 2014;219:341-59. doi: 10.1007/978-3-642-41199-1_17.

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

Author information

1
Biochemistry and Molecular Biology Graduate Program, University of California, Riverside, CA, USA.

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.

PMID:
24292838
DOI:
10.1007/978-3-642-41199-1_17
[Indexed for MEDLINE]

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