Evidence map›Paper›PMID 34241650›Full record

ArticleCellular and molecular life sciences : CMLS2021

Ligand-binding and -scavenging of the chemerin receptor GPR1.

Tobias F Fischer, Anne S Czerniak, Tina Weiß, Clara T Schoeder, Philipp Wolf, Oliver Seitz, Jens Meiler, Annette G Beck-Sickinger

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

17 citing papers in PubMed, 23 citations in OpenAlex.

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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

8 authors at 4 institutions in 2 countries.

Tobias F FischerInstitute of Biochemistry, Leipzig University, Brüderstraße 34, 04103, Leipzig, Germany.
Anne S CzerniakInstitute of Biochemistry, Leipzig University, Brüderstraße 34, 04103, Leipzig, Germany.
Tina WeißInstitute of Biochemistry, Leipzig University, Brüderstraße 34, 04103, Leipzig, Germany.
Clara T SchoederCenter for Structural Biology, Department of Chemistry, Vanderbilt University, 465 21st Avenue South, Nashville, TN37212, USA.
Philipp WolfInstitute of Biochemistry, Leipzig University, Brüderstraße 34, 04103, Leipzig, Germany.
Oliver SeitzDepartment of Chemistry, Humboldt-Universität Zu Berlin, Brook-Taylor-Str. 2, 12489, Berlin, Germany.
Jens MeilerCenter for Structural Biology, Department of Chemistry, Vanderbilt University, 465 21st Avenue South, Nashville, TN37212, USA.
Annette G Beck-SickingerInstitute of Biochemistry, Leipzig University, Brüderstraße 34, 04103, Leipzig, Germany. abeck-sickinger@uni-leipzig.de.ORCID http://orcid.org/0000-0003-4560-8020
Leipzig University · DEVanderbilt University · USHumboldt-Universität zu Berlin · DELeipzig University of Applied Sciences · DE

Funding

High-Performance Computer Cluster for Biomedical ResearchS10OD023680 · OD · VANDERBILT UNIVERSITY · PI MEILER, JENS · 2017 to 2017
$587k
Hybrid Methods for Prediction and Design of Novel Human Influenza AntibodiesR56AI110750 · NIAID · VANDERBILT UNIVERSITY · PI CROWE, JAMES E, MEILER, JENS · 2014 to 2014
$433k
NIAID NIH HHS R56 AI110750NIH HHS S10 OD023680
6 · The paper itself

Abstract

Tight regulation of cytokines is essential for the initiation and resolution of inflammation. Chemerin, a mediator of innate immunity, mainly acts on chemokine-like receptor 1 (CMKLR1) to induce the migration of macrophages and dendritic cells. The role of the second chemerin receptor, G protein-coupled receptor 1 (GPR1), is still unclear. Here we demonstrate that GPR1 shows ligand-induced arrestin3 recruitment and internalization. The chemerin C-terminus triggers this activation by folding into a loop structure, binding to aromatic residues in the extracellular loops of GPR1. While this overall binding mode is shared between GPR1 and CMKLR1, differences in their respective extracellular loop 2 allowed for the design of the first GPR1-selective peptide. However, our results suggest that ligand-induced arrestin recruitment is not the only mode of action of GPR1. This receptor also displays constitutive internalization, which allows GPR1 to internalize inactive peptides efficiently by an activation-independent pathway. Our results demonstrate that GPR1 takes a dual role in regulating chemerin activity: as a signaling receptor for arrestin-based signaling on one hand, and as a scavenging receptor with broader ligand specificity on the other.

Indexed as

LigandsArrestinsBinding SitesChemokinesFluorescence Resonance Energy TransferHEK293 CellsHumansImmunity, InnateMicroscopy, ConfocalMolecular Docking SimulationMutagenesisPeptidesProtein BindingProtein Structure, TertiaryReceptors, ChemokineReceptors, G-Protein-Coupledarrestin3ArrestinsChemokinesCMKLR1 protein, humanGPR1 protein, humanLigandsPeptidesRARRES2 protein, humanReceptors, ChemokineReceptors, G-Protein-CoupledAdipokineAtypical chemokine receptorGPCRInflammation

Identifiers

PMID34241650
PMCPMC8429170
OpenAlexW3178420486

What OpenQuestion holds

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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.