Evidence map›Paper›PMID 29180449›Full record

ArticleThe Journal of biological chemistry2018

Ligand-specific conformational transitions and intracellular transport are required for atypical chemokine receptor 3-mediated chemokine scavenging.

Nicolas Montpas, Geneviève St-Onge, Nassr Nama, David Rhainds, Besma Benredjem, Mélanie Girard, Gilles Hickson, Véronique Pons, Nikolaus Heveker

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.7field-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

27 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Atypical chemokine receptors in the immune system.Nature reviews. Immunology · 2024
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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

9 authors at 2 institutions in 2 countries.

Nicolas MontpasFrom the Department of Biochemistry and Molecular Medicine, University of Montréal, Montréal, Quebec H3T 1J4, Canada.ORCID 0000-0003-4190-9424
Geneviève St-Ongethe Research Centre, Saint-Justine Hospital, University of Montréal, Montréal, Quebec H3T 1C5, Canada.
Nassr NamaFrom the Department of Biochemistry and Molecular Medicine, University of Montréal, Montréal, Quebec H3T 1J4, Canada.
David RhaindsFrom the Department of Biochemistry and Molecular Medicine, University of Montréal, Montréal, Quebec H3T 1J4, Canada.
Besma BenredjemFrom the Department of Biochemistry and Molecular Medicine, University of Montréal, Montréal, Quebec H3T 1J4, Canada.
Mélanie GirardFrom the Department of Biochemistry and Molecular Medicine, University of Montréal, Montréal, Quebec H3T 1J4, Canada.
Gilles Hicksonthe Research Centre, Saint-Justine Hospital, University of Montréal, Montréal, Quebec H3T 1C5, Canada.
Véronique PonsINSERM, UMR 1048, Institut des Maladies Métaboliques et Cardiovasculaires, Université de Toulouse, F-31432 Toulouse, France.
Nikolaus HevekerFrom the Department of Biochemistry and Molecular Medicine, University of Montréal, Montréal, Quebec H3T 1J4, Canada, nikolaus.heveker@recherche-ste-justine.qc.ca.
Centre Hospitalier Universitaire Sainte-Justine · CAInserm · FR

Funding

CIHR MOP123421
6 · The paper itself

Abstract

The atypical chemokine receptor ACKR3 contributes to chemotaxis by binding, internalizing, and degrading the chemokines CXCL11 and CXCL12 to shape and terminate chemotactic gradients during development and immune responses. Although unable to trigger G protein activation, both ligands activate G protein-independent ACKR3 responses and prompt arrestin recruitment. This offers a model to specifically study ligand-specific receptor conformations leading to G protein-independent signaling and to functional parameters such as receptor transport and chemokine degradation. We here show chemokine specificity in arrestin recruitment, by different effects of single amino acid substitutions in ACKR3 on arrestin in response to CXCL12 or CXCL11. Chemokine specificity in receptor transport was also observed, as CXCL11 induced faster receptor internalization, slower recycling, and longer intracellular sojourn of ACKR3 than CXCL12. Internalization and recycling rates of the ACKR3 R142

Indexed as

ArrestinChemokine CXCL11Chemokine CXCL12Flow CytometryHEK293 CellsHumansMicroscopy, ConfocalMutationProtein BindingReceptors, CXCRSignal TransductionACKR3 protein, humanArrestinChemokine CXCL11Chemokine CXCL12CXCL11 protein, humanCXCL12 protein, humanReceptors, CXCRACKR3arrestinarrestin recruitmentatypical chemokine receptorbioluminescence resonance energy transfer (BRET)chemokinechemokine scavengingCXCL11CXCL12CXCR7I-TACligandreceptorreceptor endocytosisreceptor recyclingreceptor transportSDF-1structure-function

Identifiers

PMID29180449
PMCPMC5777261
OpenAlexW2769686732

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.