Evidence map›Paper›PMID 24680424›Full record

ReviewCurrent opinion in cell biology2014

Extensive shape shifting underlies functional versatility of arrestins.

Vsevolod V Gurevich, Eugenia V Gurevich

Abstract readReview
In one paragraph

Review in Current opinion in cell biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.8field-weighted citation impact, top 15% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

26 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Arrestins as Possible Drug Targets.Biomolecules & therapeutics · 2025
    Review
  3. Assembling the jigsaw puzzle of life.Trends in biochemical sciences · 2025
    Article
  4. Article
  5. Arrestins: A Small Family of Multi-Functional Proteins.International journal of molecular sciences · 2024
    Review
  6. Pharmacological reviews · 2023
    Review
  7. Article
  8. G protein-coupled receptor signaling: transducers and effectors.American journal of physiology. Cell physiology · 2022
    Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Arrestins: Introducing Signaling Bias Into Multifunctional Proteins.Progress in molecular biology and translational science · 2018
    Review
  14. Molecular Mechanisms of GPCR Signaling: A Structural Perspective.International journal of molecular sciences · 2017
    Review
  15. Hepatic β-arrestin 2 is essential for maintaining euglycemia.The Journal of clinical investigation · 2017
    Article
  16. Article
  17. Article
  18. Article
  19. A Comprehensive View of the β-Arrestinome.Frontiers in endocrinology · 2017
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Vsevolod V GurevichDepartment of Pharmacology, Vanderbilt University, Nashville, TN 37232, USA. Electronic address: vsevolod.gurevich@vanderbilt.edu.
Eugenia V GurevichDepartment of Pharmacology, Vanderbilt University, Nashville, TN 37232, USA.
Vanderbilt University · US

Funding

STRUCTURE/FUNCTION STUDIES OF VISUAL ARRESTINR01EY011500 · NEI · VANDERBILT UNIVERSITY · PI T M Iverson · 1997 to 2026
$12.3M
Arrestin interactions with non-receptor binding partnersR01GM077561 · NIGMS · VANDERBILT UNIVERSITY · PI GUREVICH, VSEVOLOD V. · 2007 to 2015
$2.3M
Signaling regulation in the striatum in Parkinson's diseaseR01NS065868 · NINDS · VANDERBILT UNIVERSITY · PI GUREVICH, EUGENIA V · 2009 to 2013
$1.7M
Conformational regulation of arrestin-mediated signalingR01GM081756 · NIGMS · VANDERBILT UNIVERSITY · PI GUREVICH, VSEVOLOD V. · 2008 to 2011
$1.5M
The role of receptor desensitization machinery in psychostimulant addictionR21DA030103 · NIDA · VANDERBILT UNIVERSITY · PI GUREVICH, EUGENIA V · 2011 to 2012
$390k
NEI NIH HHS EY011500NEI NIH HHS R01 EY011500NIDA NIH HHS DA030103NIDA NIH HHS R21 DA030103NIGMS NIH HHS GM077561NIGMS NIH HHS GM081756NIGMS NIH HHS R01 GM077561NIGMS NIH HHS R01 GM081756NINDS NIH HHS NS065868NINDS NIH HHS R01 NS065868
6 · The paper itself

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.

Indexed as

AnimalsArrestinsHumansPhosphorylationProtein BindingProtein ConformationReceptors, G-Protein-CoupledSignal TransductionArrestinsReceptors, G-Protein-Coupled

Identifiers

PMID24680424
PMCPMC3971385
OpenAlexW2043111450

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.