Evidence map›Paper›PMID 23471539›Full record

ReviewMolecular endocrinology (Baltimore, Md.)2013

Minireview: ubiquitination-regulated G protein-coupled receptor signaling and trafficking.

Verónica Alonso, Peter A Friedman

Open access · bronzeAbstract readReview
In one paragraph

Review in Molecular endocrinology (Baltimore, Md.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

27 citing papers in PubMed, 63 citations in OpenAlex.

  1. Review
  2. Article
  3. Proteasomal-dependent endothelial P2YPurinergic signalling · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Review
  10. Posttranslational modifications in proteins: resources, tools and prediction methods.Database : the journal of biological databases and curation · 2021
    Article
  11. Review
  12. Review
  13. Article
  14. Cell Clearing Systems Bridging Neuro-Immunity and Synaptic Plasticity.International journal of molecular sciences · 2019
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Regulation of G Protein-Coupled Receptors by Ubiquitination.International journal of molecular sciences · 2017
    Review
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 2 institutions in 2 countries.

Verónica AlonsoInstitute of Applied Molecular Medicine, San Pablo-CEU University School of Medicine, Madrid, 28668, Spain.
Peter A Friedman
Universidad San Pablo CEU · ESUniversity of Pittsburgh · US

Funding

PTH Receptor: Posttranslational Modification and Recycling in BoneR01DK054171 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI FRIEDMAN, PETER A · 1998 to 2015
$6.0M
EBP50 REGULATION OF PTH RECEPTOR IN BONE AND KIDNEYR01DK069998 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI FRIEDMAN, PETER A · 2006 to 2014
$2.9M
NIDDK NIH HHS DK054171NIDDK NIH HHS DK069998NIDDK NIH HHS R01 DK054171NIDDK NIH HHS R01 DK069998
6 · The paper itself

Abstract

G protein-coupled receptors (GPCRs) are the largest and most diverse superfamily of membrane proteins and mediate most cellular responses to hormones and neurotransmitters. Posttranslational modifications are considered the main regulators of all GPCRs. In addition to phosphorylation, glycosylation, and palmitoylation, increasing evidence as reviewed here reveals that ubiquitination also regulates the magnitude and temporospatial aspects of GPCR signaling. Posttranslational protein modification by ubiquitin is a key molecular mechanism governing proteins degradation. Ubiquitination mediates the covalent conjugation of ubiquitin, a highly conserved polypeptide of 76 amino acids, to protein substrates. This process is catalyzed by 3 enzymes acting in tandem: an E1, ubiquitin-activating enzyme; an E2, ubiquitin-carrying enzyme; and an E3, ubiquitin ligase. Ubiquitination is counteracted by deubiquitinating enzymes that deconjugate ubiquitin-modified proteins and rescue the substrate from proteasomal degradation. Although ubiquitination is known to target many GPCRs for lysosomal or proteasomal degradation, emerging findings define novel roles for the basal status of ubiquitination and for rapid deubiquitination and transubiquitination controlling cell surface expression and cellular responsiveness of some GPCRs. In this review, we highlight the classical and novel roles of ubiquitin in the regulation of GPCR function, signaling, and trafficking.

Indexed as

Signal TransductionUbiquitinationAnimalsDiseaseHumansProtein Processing, Post-TranslationalProtein TransportReceptors, G-Protein-CoupledReceptors, G-Protein-Coupled

Identifiers

PMID23471539
PMCPMC3607699
OpenAlexW1995220259

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.