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PMID: 24680424 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Review

Extensive shape shifting underlies functional versatility of arrestins.

Current opinion in cell biology ·Vol. 27 ·2014-04-00 ·Pages 1-9

Gurevich VV, Gurevich EV

Abstract

Among four vertebrate arrestins, only two are ubiquitously expressed. Arrestins specifically bind active phosphorylated G protein-coupled receptors (GPCRs), thereby precluding further G protein activation. Recent discoveries suggest that the formation of the arrestin-receptor complex initiates the second round of signaling with comparable biological importance. Despite having virtually no recognizable sequence motifs known to mediate protein-protein interactions, arrestins bind a surprising variety of signaling proteins with mind-boggling range of functional consequences. High conformational flexibility allows arrestins to show many distinct 'faces' to the world, which allows these relatively small ∼45kDa proteins to bind various partners under different physiological conditions, organizing multi-protein signaling complexes and localizing them to distinct subcellular compartments.

MeSH Terms
Animals Arrestins/chemistry,metabolism Humans Phosphorylation Protein Binding Protein Conformation Receptors, G-Protein-Coupled/metabolism Signal Transduction
Chemicals
Arrestins Receptors, G-Protein-Coupled
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Gurevich Vsevolod V
Department of Pharmacology, Vanderbilt University, Nashville, TN 37232, USA. Electronic address: vsevolod.gurevich@vanderbilt.edu.
Gurevich Eugenia V
Department of Pharmacology, Vanderbilt University, Nashville, TN 37232, USA.
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Article Info
Journal
Current opinion in cell biology
Abbr.
Curr Opin Cell Biol
ISSN
1879-0410
DOI
10.1016/j.ceb.2013.10.007
Email
vsevolod.gurevich@vanderbilt.edu
Published
2014-04-00
Epub
2013-00-16
Pages
1-9
Language
English
Region
England
NLM ID
8913428
PMCID
PMC3971385
Subset
IM
Grants
NIGMS NIH HHS · GM081756 · United States
NIDA NIH HHS · DA030103 · United States
NIGMS NIH HHS · R01 GM077561 · United States
NIGMS NIH HHS · R01 GM081756 · United States
NINDS NIH HHS · NS065868 · United States
NEI NIH HHS · EY011500 · United States
NEI NIH HHS · R01 EY011500 · United States
NINDS NIH HHS · R01 NS065868 · United States
NIGMS NIH HHS · GM077561 · United States
NIDA NIH HHS · R21 DA030103 · United States
External Links
PubMed source DOI: 10.1016/j.ceb.2013.10.007 PMC Full Text View journal details
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