Evidence map›Paper›PMID 22938866›Full record

ArticleCell reports2012

The GPS motif is a molecular switch for bimodal activities of adhesion class G protein-coupled receptors.

Simone Prömel, Marie Frickenhaus, Samantha Hughes, Lamia Mestek, David Staunton, Alison Woollard, Ioannis Vakonakis, Torsten Schöneberg, Ralf Schnabel, Andreas P Russ and 1 more

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Cell reports, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

81 citing papers in PubMed, 145 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Adhesion G protein-coupled receptors.Pharmacological reviews · 2026
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Bacterial SEAL domains undergo autoproteolysis and function in regulated intramembrane proteolysis.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article

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

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

11 authors at 3 institutions in 2 countries.

Simone PrömelDepartment of Biochemistry, University of Oxford, UK.
Marie Frickenhaus
Samantha Hughes
Lamia Mestek
David Staunton
Alison Woollard
Ioannis Vakonakis
Torsten Schöneberg
Ralf Schnabel
Andreas P Russ
Tobias Langenhan
University of Oxford · GBLeipzig University · DETechnische Universität Braunschweig · DE

Funding

Biotechnology and Biological Sciences Research Council BB/C504200/1Wellcome TrustWellcome Trust WT075336/Z/04/A
6 · The paper itself

Abstract

Adhesion class G protein-coupled receptors (aGPCR) form the second largest group of seven-transmembrane-spanning (7TM) receptors whose molecular layout and function differ from canonical 7TM receptors. Despite their essential roles in immunity, tumorigenesis, and development, the mechanisms of aGPCR activation and signal transduction have remained obscure to date. Here, we use a transgenic assay to define the protein domains required in vivo for the activity of the prototypical aGPCR LAT-1/Latrophilin in Caenorhabditis elegans. We show that the GPCR proteolytic site (GPS) motif, the molecular hallmark feature of the entire aGPCR class, is essential for LAT-1 signaling serving in two different activity modes of the receptor. Surprisingly, neither mode requires cleavage but presence of the GPS, which relays interactions with at least two different partners. Our work thus uncovers the versatile nature of aGPCR activity in molecular detail and places the GPS motif in a central position for diverse protein-protein interactions.

Indexed as

Amino Acid MotifsAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsReceptors, G-Protein-CoupledReceptors, PeptideSignal TransductionCaenorhabditis elegans Proteinslat-1 protein, C elegansReceptors, G-Protein-CoupledReceptors, Peptide

Identifiers

PMID22938866
PMCPMC3776922
OpenAlexW1977789280

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.