Evidence map›Paper›PMID 31502283›Full record

ArticleAnnals of the New York Academy of Sciences2019

Spatial regulation of GPR64/ADGRG2 signaling by β-arrestins and GPCR kinases.

Pedram Azimzadeh, Sarah C Talamantez-Lyburn, Katarina T Chang, Asuka Inoue, Nariman Balenga

Open access · greenAbstract read
In one paragraph

Article in Annals of the New York Academy of Sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

16 citing papers in PubMed, 25 citations in OpenAlex.

  1. Adhesion G protein-coupled receptors.Pharmacological reviews · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Structures of the ADGRG2-GNature chemical biology · 2022
    Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Mechanisms of adhesion G protein-coupled receptor activation.The Journal of biological chemistry · 2020
    Review
  13. Review
  14. Review
  15. The Emerging Role of Adhesion GPCRs in Cancer.ACS pharmacology & translational science · 2020
    Review
  16. 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

5 authors at 3 institutions in 2 countries.

Pedram AzimzadehDivision of General and Oncologic Surgery, Department of Surgery, University of Maryland School of Medicine, Baltimore, Maryland.
Sarah C Talamantez-LyburnGraduate Program in Life Sciences, University of Maryland, Baltimore, Maryland.
Katarina T ChangGraduate Program in Life Sciences, University of Maryland, Baltimore, Maryland.
Asuka InoueGraduate School of Pharmaceutical Sciences, Tohoku University, Sendai, Japan.
Nariman BalengaDivision of General and Oncologic Surgery, Department of Surgery, University of Maryland School of Medicine, Baltimore, Maryland.
University of Maryland, Baltimore · USTohoku University · JPUniversity of Maryland Marlene and Stewart Greenebaum Comprehensive Cancer Center

Funding

EXPAND PARTICIPATION BY MINORITIES IN BIOMEDICAL SCIENCER25GM055036 · NIGMS · UNIVERSITY OF MARYLAND BALTIMORE COUNTY · PI SUMMERS, MICHAEL FINLEY · 1996 to 2021
$16.9M
Mechanisms of activation, signaling and trafficking of adhesion GPCRs GPR64 and GPR56R01GM130617 · NIGMS · UNIVERSITY OF MARYLAND BALTIMORE · PI OLSON, JOHN A. · 2019 to 2021
$1.0M
NIGMS NIH HHS R01 GM130617NIGMS NIH HHS R25 GM055036
6 · The paper itself

Abstract

Mechanisms of activation, signaling, and trafficking of adhesion G protein-coupled receptors (aGPCRs) have remained largely unknown. Several aGPCRs, including GPR56/ADGRG1 and GPR64/ADGRG2, show increased activity in the absence of their N-terminal fragment (NTF). This constitutive signaling is plausibly caused by the binding of extracellular N-terminal 15-25 amino acid-long tethered agonist to extracellular domains of the cognate aGPCRs. To test the role of NTF and tethered agonist in GPR64 signaling and endocytosis, we generated mutants that lack either NTF alone (ΔNTF) or NTF and tethered agonist (P622). We discover that unlike full-length GPR64, ΔNTF and P622 mutants interact with β-arrestin1 and β-arrestins2 and are constitutively internalized in steady states. However, only ΔNTF shows exaggerated basal activation of the Gα

Indexed as

Signal Transductionbeta-ArrestinsDynaminsEndocytosisEndosomesHEK293 CellsHumansProtein KinasesProtein TransportReceptors, G-Protein-CoupledADGRG1 protein, humanADGRG2 protein, humanbeta-ArrestinsDynaminsProtein KinasesReceptors, G-Protein-Coupledadhesion GPCRendocytosisGPCR kinaseG protein

Identifiers

PMID31502283
PMCPMC7236788
OpenAlexW2973086015

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.