Evidence map›Paper›PMID 29078385›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

GPCRs globally coevolved with receptor activity-modifying proteins, RAMPs.

Shahar Barbash, Emily Lorenzen, Torbjörn Persson, Thomas Huber, Thomas P Sakmar

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Gas-sensing riboceptors.RNA biology · 2024
    Article
  3. Article
  4. Expanding the GPCR-RAMP interactome.bioRxiv : the preprint server for biology · 2023
    Article
  5. Review
  6. Review
  7. Functional modulation of PTH1R activation and signaling by RAMP2.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Article
  9. Article
  10. Dawn of a New RAMPage.Trends in pharmacological sciences · 2020
    Review
  11. Review
  12. RAMP3 determines rapid recycling of atypical chemokine receptor-3 for guided angiogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. 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 2 institutions in 2 countries.

Shahar BarbashLaboratory of Chemical Biology and Signal Transduction, The Rockefeller University, New York, NY, 10065.
Emily LorenzenLaboratory of Chemical Biology and Signal Transduction, The Rockefeller University, New York, NY, 10065.
Torbjörn PerssonLaboratory of Chemical Biology and Signal Transduction, The Rockefeller University, New York, NY, 10065.
Thomas HuberLaboratory of Chemical Biology and Signal Transduction, The Rockefeller University, New York, NY, 10065; hubert@rockefeller.edu sakmar@rockefeller.edu.
Thomas P SakmarLaboratory of Chemical Biology and Signal Transduction, The Rockefeller University, New York, NY, 10065; hubert@rockefeller.edu sakmar@rockefeller.edu.ORCID 0000-0002-2836-8953
Rockefeller University · USKarolinska Institutet · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Receptor activity-modifying proteins (RAMPs) are widely expressed in human tissues and, in some cases, have been shown to affect surface expression or ligand specificity of G-protein-coupled receptors (GPCRs). However, whether RAMP-GPCR interactions are widespread, and the nature of their functional consequences, remains largely unknown. In humans, there are three RAMPs and over 800 expressed GPCRs, making direct experimental approaches challenging. We analyzed relevant genomic data from all currently available sequenced organisms. We discovered that RAMPs and GPCRs tend to have orthologs in the same species and have correlated phylogenetic trees to the same extent, or higher than other interacting protein pairs that play key roles in cellular signaling. In addition, the resulting RAMP-GPCR interaction map suggests that RAMP1 and RAMP3 interact with the same set of GPCRs, which implies functional redundancy. We next analyzed human transcriptomes and found expression correlation for GPCRs and RAMPs. Our results suggest global coevolution of GPCRs and RAMPS and support the hypothesis that GPCRs interact globally with RAMPs in cellular signaling pathways.

Indexed as

Amino Acid SequenceHumansLigandsMembrane ProteinsPhylogenyProtein BindingReceptor Activity-Modifying ProteinsReceptors, G-Protein-CoupledSignal TransductionTranscriptomeLigandsMembrane ProteinsReceptor Activity-Modifying ProteinsReceptors, G-Protein-CoupledcoevolutionG-protein–coupled receptorphylogenetic analysisreceptor activity-modifying proteinsignal transduction

Identifiers

PMID29078385
PMCPMC5692586
OpenAlexW2765472374

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.