Evidence map›Paper›PMID 31555726›Full record

ArticleScience advances2019

Multiplexed analysis of the secretin-like GPCR-RAMP interactome.

Emily Lorenzen, Tea Dodig-Crnković, Ilana B Kotliar, Elisa Pin, Emilie Ceraudo, Roger D Vaughan, Mathias Uhlèn, Thomas Huber, Jochen M Schwenk, Thomas P Sakmar

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

46 citing papers in PubMed, 83 citations in OpenAlex.

  1. Signaling architecture of the glucagon-like peptide-1 receptor.The Journal of clinical investigation · 2026
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  18. Expanding the GPCR-RAMP interactome.bioRxiv : the preprint server for biology · 2023
    Article
  19. Review
  20. 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

10 authors at 4 institutions in 2 countries.

Emily LorenzenLaboratory of Chemical Biology and Signal Transduction, The Rockefeller University, 1230 York Ave., New York, NY 10065, USA.ORCID 0000-0002-0008-0966
Tea Dodig-CrnkovićScience for Life Laboratory, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of Technology, 171 65 Solna, Sweden.ORCID 0000-0002-2875-896X
Ilana B KotliarLaboratory of Chemical Biology and Signal Transduction, The Rockefeller University, 1230 York Ave., New York, NY 10065, USA.ORCID 0000-0001-9533-4828
Elisa PinScience for Life Laboratory, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of Technology, 171 65 Solna, Sweden.ORCID 0000-0002-2158-2674
Emilie CeraudoLaboratory of Chemical Biology and Signal Transduction, The Rockefeller University, 1230 York Ave., New York, NY 10065, USA.ORCID 0000-0001-6563-9751
Roger D VaughanCenter for Clinical and Translational Science, The Rockefeller University, 1230 York Ave., New York, NY 10065, USA.
Mathias UhlènScience for Life Laboratory, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of Technology, 171 65 Solna, Sweden.ORCID 0000-0002-4858-8056
Thomas HuberLaboratory of Chemical Biology and Signal Transduction, The Rockefeller University, 1230 York Ave., New York, NY 10065, USA.ORCID 0000-0002-1844-262X
Jochen M SchwenkScience for Life Laboratory, School of Engineering Sciences in Chemistry, Biotechnology and Health, KTH Royal Institute of Technology, 171 65 Solna, Sweden.ORCID 0000-0001-8141-8449
Thomas P SakmarLaboratory of Chemical Biology and Signal Transduction, The Rockefeller University, 1230 York Ave., New York, NY 10065, USA.ORCID 0000-0002-2836-8953
Rockefeller University · USScience for Life Laboratory · SEKarolinska Institutet · SETri-Institutional PhD Program in Chemical Biology · US

Funding

Tri-Institutional PhD Program in Chemical BiologyT32GM136640 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI DEREK S TAN · 2020 to 2026
$2.4M
NIGMS NIH HHS T32 GM136640
6 · The paper itself

Abstract

Receptor activity-modifying proteins (RAMPs) have been shown to modulate the functions of several G protein-coupled receptors (GPCRs), but potential direct interactions among the three known RAMPs and hundreds of GPCRs have never been investigated. Focusing mainly on the secretin-like family of GPCRs, we engineered epitope-tagged GPCRs and RAMPs, and developed a multiplexed suspension bead array (SBA) immunoassay to detect GPCR-RAMP complexes from detergent-solubilized lysates. Using 64 antibodies raised against the native proteins and 4 antibodies targeting the epitope tags, we mapped the interactions among 23 GPCRs and 3 RAMPs. We validated nearly all previously reported secretin-like GPCR-RAMP interactions, and also found previously unidentified RAMP interactions with additional secretin-like GPCRs, chemokine receptors, and orphan receptors. The results provide a complete interactome of secretin-like GPCRs with RAMPs. The SBA strategy will be useful to search for additional GPCR-RAMP complexes and other interacting membrane protein pairs in cell lines and tissues.

Indexed as

Protein Interaction MappingHEK293 CellsHumansReceptor Activity-Modifying ProteinsReceptors, G-Protein-CoupledSecretinReceptor Activity-Modifying ProteinsReceptors, G-Protein-CoupledSecretin

Identifiers

PMID31555726
PMCPMC6750928
OpenAlexW2973504822

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.