Evidence map›Paper›PMID 28424266›Full record

ArticleThe Journal of biological chemistry2017

Disease-associated extracellular loop mutations in the adhesion G protein-coupled receptor G1 (ADGRG1; GPR56) differentially regulate downstream signaling.

Ayush Kishore, Randy A Hall

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Adhesion G protein-coupled receptors.Pharmacological reviews · 2026
    Review
  3. Review
  4. Article
  5. Mechanism of tethered agonist-mediated signaling by polycystin-1.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Mechanisms of adhesion G protein-coupled receptor activation.The Journal of biological chemistry · 2020
    Review
  13. Review
  14. Article
  15. Article
  16. Review
  17. Teneurins and latrophilins: two giants meet at the synapse.Current opinion in structural biology · 2019
    Review
  18. Article
  19. Article
  20. Proceedings of the National Academy of Sciences of the United States of America · 2017
    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.

Ayush KishoreFrom the Department of Pharmacology, Emory University School of Medicine, Atlanta, Georgia 30322.
Randy A HallFrom the Department of Pharmacology, Emory University School of Medicine, Atlanta, Georgia 30322 rhall3@emory.edu.ORCID 0000-0002-8318-8728
Emory University · US

Funding

Graduate Training in the Pharmacological StudiesT32GM008602 · NIGMS · EMORY UNIVERSITY · PI HALL, RANDY A. · 1996 to 2021
$5.1M
Activation and regulation of the neural stem cell-expressed receptor GPR56R01NS072394 · NINDS · EMORY UNIVERSITY · PI HALL, RANDY A. · 2011 to 2015
$1.7M
NIGMS NIH HHS T32 GM008602NINDS NIH HHS R01 NS072394
6 · The paper itself

Abstract

Mutations to the adhesion G protein-coupled receptor ADGRG1 (G1; also known as GPR56) underlie the neurological disorder bilateral frontoparietal polymicrogyria. Disease-associated mutations in G1 studied to date are believed to induce complete loss of receptor function through disruption of either receptor trafficking or signaling activity. Given that N-terminal truncation of G1 and other adhesion G protein-coupled receptors has been shown to significantly increase the receptors' constitutive signaling, we examined two different bilateral frontoparietal polymicrogyria-inducing extracellular loop mutations (R565W and L640R) in the context of both full-length and N-terminally truncated (ΔNT) G1. Interestingly, we found that these mutations reduced surface expression of full-length G1 but not G1-ΔNT in HEK-293 cells. Moreover, the mutations ablated receptor-mediated activation of serum response factor luciferase, a classic measure of Gα

Indexed as

Mutation, MissenseSignal TransductionAmino Acid Substitutionbeta-Arrestin 1Cell LineGTP-Binding Protein alpha Subunits, G12-G13GTP-Binding Protein beta SubunitsGTP-Binding Protein gamma SubunitsHumansMalformations of Cortical DevelopmentProtein Structure, SecondaryProtein TransportReceptors, G-Protein-CoupledADGRG1 protein, humanARRB1 protein, humanbeta-Arrestin 1GTP-Binding Protein alpha Subunits, G12-G13GTP-Binding Protein beta SubunitsGTP-Binding Protein gamma SubunitsReceptors, G-Protein-CoupledarrestinG protein-coupled receptor (GPCR)ion channelreceptorsignal transduction

Identifiers

PMID28424266
PMCPMC5465494
OpenAlexW2605402851

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.