Evidence map›Paper›PMID 12959637›Full record

ReviewThe Biochemical journal2003

Multifaceted roles of beta-arrestins in the regulation of seven-membrane-spanning receptor trafficking and signalling.

Sudha K Shenoy, Robert J Lefkowitz

Open access · bronzeAbstract readReview
In one paragraph

Review in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 139 papers.

0numbers the graph read from it
0cells of the map it votes in
139citing papers in PubMed
12.1field-weighted citation impact, top 1% 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

139 citing papers in PubMed, 405 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
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  6. Review
  7. Review
  8. Article
  9. Article
  10. Arrestin-3 Agonism at Dopamine DBiological psychiatry · 2023
    Article
  11. GPCR targeting of E3 ubiquitin ligase MDM2 by inactive β-arrestin.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Review

79 more citing papers are in PubMed but not listed here.

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.

Sudha K ShenoyDepartment of Medicine, Howard Hughes Medical Institute, Duke University Medical Center, Box 3821, Durham, NC 27710, USA.
Robert J Lefkowitz
Howard Hughes Medical Institute · US

Funding

Molecular Regulation of Cardiovascular 7 TM ReceptorsR01HL016037 · NHLBI · DUKE UNIVERSITY · PI ROBERT J LEFKOWITZ · 1985 to 2026
$14.5M
B-Arrestins and G Protein-Coupled Receptor Kinases in Cardiovascular FunctionR01HL070631 · NHLBI · DUKE UNIVERSITY · PI LEFKOWITZ, ROBERT J · 2002 to 2011
$3.5M
MOLECULAR PROPERTIES OF CARDIAC ADRENERGIC RECEPTORSR37HL016037 · NHLBI · DUKE UNIVERSITY · PI LEFKOWITZ, ROBERT J · 1986 to 1995
–
NHLBI NIH HHS HL16037NHLBI NIH HHS HL70631
6 · The paper itself

Abstract

Beta-arrestins are cytosolic proteins that bind to activated and phosphorylated G-protein-coupled receptors [7MSRs (seven-membrane-spanning receptors)] and uncouple them from G-protein-mediated second messenger signalling pathways. The binding of beta-arrestins to 7MSRs also leads to new signals via activation of MAPKs (mitogen-activated protein kinases) such as JNK3 (c-Jun N-terminal kinase 3), ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38 MAPKs. By binding to endocytic proteins [clathrin, AP2 (adapter protein 2), NSF (N -ethylmaleimide-sensitive fusion protein) and ARF6 (ADP-ribosylation factor 6)], beta-arrestins also serve as adapters to link the receptors to the cellular trafficking machinery. Agonist-promoted ubiquitination of beta-arrestins is a prerequisite for their role in receptor internalization, as well as a determinant of the differing trafficking patterns of distinct classes of receptors. Recently, beta-arrestins have also been implicated as playing novel roles in cellular chemotaxis and apoptosis. By virtue of their ability to bind, in a stimulus-dependent fashion, to 7MSRs as well as to different classes of cellular proteins, beta-arrestins serve as versatile adapter proteins that regulate the signalling and trafficking of the receptors.

Indexed as

ADP-Ribosylation Factor 6AnimalsArrestinsbeta-ArrestinsBiological TransportEndocytosisHumansModels, BiologicalReceptors, G-Protein-CoupledSignal TransductionADP-Ribosylation Factor 6ARF6 protein, humanArrestinsbeta-ArrestinsReceptors, G-Protein-Coupled

Identifiers

PMID12959637
PMCPMC1223736
OpenAlexW2070793709

What OpenQuestion holds

Textmetadata
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.