Evidence map›Paper›PMID 28298427›Full record

ArticleMolecular systems biology2017

Systematic protein-protein interaction mapping for clinically relevant human GPCRs.

Kate Sokolina, Saranya Kittanakom, Jamie Snider, Max Kotlyar, Pascal Maurice, Jorge Gandía, Abla Benleulmi-Chaachoua, Kenjiro Tadagaki, Atsuro Oishi, Victoria Wong and 18 more

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Molecular systems biology, 2017. 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 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing 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

42 citing papers in PubMed, 69 citations in OpenAlex.

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  8. Kelch-like proteins in the gastrointestinal tumors.Acta pharmacologica Sinica · 2023
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  12. Mouse Mutants ofInternational journal of molecular sciences · 2022
    Review
  13. Review
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  16. Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

28 authors at 8 institutions in 6 countries.

Kate SokolinaDonnelly Centre, University of Toronto, Toronto, ON, Canada.
Saranya KittanakomDonnelly Centre, University of Toronto, Toronto, ON, Canada.
Jamie SniderDonnelly Centre, University of Toronto, Toronto, ON, Canada.
Max KotlyarPrincess Margaret Cancer Centre, University Health Network, University of Toronto, Toronto, ON, Canada.
Pascal MauriceInserm, U1016, Institut Cochin, Paris, France.ORCID 0000-0003-2167-4808
Jorge GandíaUnitat de Farmacologia, Departament de Patologia i Terapèutica Experimental, Facultat de Medicina, IDIBELL, Universitat de Barcelona, L'Hospitalet de Llobregat, Barcelona, Spain.ORCID 0000-0003-1711-8075
Abla Benleulmi-ChaachouaInserm, U1016, Institut Cochin, Paris, France.
Kenjiro TadagakiInserm, U1016, Institut Cochin, Paris, France.
Atsuro OishiInserm, U1016, Institut Cochin, Paris, France.
Victoria WongDonnelly Centre, University of Toronto, Toronto, ON, Canada.
Ramy H MaltyDepartment of Biochemistry, Research and Innovation Centre, University of Regina, Regina, SK, Canada.
Viktor DeinekoDepartment of Biochemistry, Research and Innovation Centre, University of Regina, Regina, SK, Canada.
Hiroyuki AokiDepartment of Biochemistry, Research and Innovation Centre, University of Regina, Regina, SK, Canada.
Shahreen AminDepartment of Biochemistry, Research and Innovation Centre, University of Regina, Regina, SK, Canada.
Zhong YaoDonnelly Centre, University of Toronto, Toronto, ON, Canada.
Xavier MoratóUnitat de Farmacologia, Departament de Patologia i Terapèutica Experimental, Facultat de Medicina, IDIBELL, Universitat de Barcelona, L'Hospitalet de Llobregat, Barcelona, Spain.
David OtasekPrincess Margaret Cancer Centre, University Health Network, University of Toronto, Toronto, ON, Canada.
Hiroyuki KobayashiDepartment of Biochemistry, Institute for Research in Immunology & Cancer, Université de Montréal, Montréal, QC, Canada.
Javier MenendezDonnelly Centre, University of Toronto, Toronto, ON, Canada.
Daniel AuerbachDualsystems Biotech AG, Schlieren, Switzerland.
Stephane AngersDepartment of Pharmaceutical Sciences, Leslie Dan Faculty of Pharmacy and Department of Biochemistry, Faculty of Medicine, University of Toronto, Toronto, ON, Canada.
Natasa PržuljDepartment of Computing, University College London, London, UK.
Michel BouvierDepartment of Biochemistry, Institute for Research in Immunology & Cancer, Université de Montréal, Montréal, QC, Canada.
Mohan BabuDepartment of Biochemistry, Research and Innovation Centre, University of Regina, Regina, SK, Canada.
Francisco CiruelaUnitat de Farmacologia, Departament de Patologia i Terapèutica Experimental, Facultat de Medicina, IDIBELL, Universitat de Barcelona, L'Hospitalet de Llobregat, Barcelona, Spain.
Ralf JockersInserm, U1016, Institut Cochin, Paris, France.
Igor JurisicaPrincess Margaret Cancer Centre, University Health Network, University of Toronto, Toronto, ON, Canada.ORCID 0000-0002-2507-946X
Igor StagljarDonnelly Centre, University of Toronto, Toronto, ON, Canada igor.stagljar@utoronto.ca.ORCID 0000-0002-5260-3327
University of Toronto · CADélégation Paris 5 · FRUniversity of Regina · CAInstitut d'Investigació Biomédica de Bellvitge · ESUniversity Health Network · CAInstitute for Research in Immunology and Cancer · CABiotechnology Institute Thurgau · CHUniversity College London · GB

Funding

CIHR MOP‐106527CIHR MOP 132191
6 · The paper itself

Abstract

G-protein-coupled receptors (GPCRs) are the largest family of integral membrane receptors with key roles in regulating signaling pathways targeted by therapeutics, but are difficult to study using existing proteomics technologies due to their complex biochemical features. To obtain a global view of GPCR-mediated signaling and to identify novel components of their pathways, we used a modified membrane yeast two-hybrid (MYTH) approach and identified interacting partners for 48 selected full-length human ligand-unoccupied GPCRs in their native membrane environment. The resulting GPCR interactome connects 686 proteins by 987 unique interactions, including 299 membrane proteins involved in a diverse range of cellular functions. To demonstrate the biological relevance of the GPCR interactome, we validated novel interactions of the GPR37, serotonin 5-HT4d, and adenosine ADORA2A receptors. Our data represent the first large-scale interactome mapping for human GPCRs and provide a valuable resource for the analysis of signaling pathways involving this druggable family of integral membrane proteins.

Indexed as

Protein Interaction MapsCell MembraneHumansProtein Interaction MappingReceptor, Adenosine A2AReceptors, G-Protein-CoupledReceptors, Serotonin, 5-HT4Signal TransductionTwo-Hybrid System TechniquesGPR37 receptor, humanReceptor, Adenosine A2AReceptors, G-Protein-CoupledReceptors, Serotonin, 5-HT4G‐protein‐coupled receptorshigh‐throughput screeningintegrative computational biologyinteractomeprotein–protein interactionssplit‐ubiquitin membrane yeast two‐hybrid assay

Identifiers

PMID28298427
PMCPMC5371730
OpenAlexW2602591433

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.