Document Detail


Molecular mechanisms underlying Beta-arrestin-dependent chemotaxis and actin-cytoskeletal reorganization.
MedLine Citation:
PMID:  24292838     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
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:
Kathryn W McGovern; Kathryn A Defea
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Handbook of experimental pharmacology     Volume:  219     ISSN:  0171-2004     ISO Abbreviation:  Handb Exp Pharmacol     Publication Date:  2014  
Date Detail:
Created Date:  2013-12-02     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7902231     Medline TA:  Handb Exp Pharmacol     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  341-59     Citation Subset:  IM    
Affiliation:
Biochemistry and Molecular Biology Graduate Program, University of California, Riverside, CA, USA.
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