Evidence map›Paper›PMID 33292475›Full record

ArticleCell & bioscience2020

CXCR7: a β-arrestin-biased receptor that potentiates cell migration and recruits β-arrestin2 exclusively through Gβγ subunits and GRK2.

Huong Thi Nguyen, Arfaxad Reyes-Alcaraz, Hyo Jeong Yong, Lan Phuong Nguyen, Hee-Kyung Park, Asuka Inoue, Cheol Soon Lee, Jae Young Seong, Jong-Ik Hwang

Open access · goldAbstract read
In one paragraph

Article in Cell & bioscience, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.6field-weighted citation impact, top 5% 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

44 citing papers in PubMed, 67 citations in OpenAlex.

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  18. Atypical chemokine receptors in the immune system.Nature reviews. Immunology · 2024
    Review
  19. Article
  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

9 authors at 3 institutions in 3 countries.

Huong Thi NguyenDepartment of Biomedical Sciences, College of Medicine, Korea University, Seoul, Republic of Korea.
Arfaxad Reyes-AlcarazCollege of Pharmacy, University of Houston, Houston, TX, USA.
Hyo Jeong YongDepartment of Biomedical Sciences, College of Medicine, Korea University, Seoul, Republic of Korea.
Lan Phuong NguyenDepartment of Biomedical Sciences, College of Medicine, Korea University, Seoul, Republic of Korea.
Hee-Kyung ParkDepartment of Biomedical Sciences, College of Medicine, Korea University, Seoul, Republic of Korea.
Asuka InoueGraduate School of Pharmaceutical Sciences, Tohoku University, Sendai, Japan.
Cheol Soon LeeDepartment of Biomedical Sciences, College of Medicine, Korea University, Seoul, Republic of Korea.
Jae Young SeongDepartment of Biomedical Sciences, College of Medicine, Korea University, Seoul, Republic of Korea.
Jong-Ik HwangDepartment of Biomedical Sciences, College of Medicine, Korea University, Seoul, Republic of Korea. hjibio@korea.ac.kr.ORCID http://orcid.org/0000-0002-0729-1782
Korea University · KRTohoku University · JPUniversity of Houston · US

Funding

Korea research foundation Grant (KR) NRF-2019R1A2C1090051
6 · The paper itself

Abstract

backgroundSome chemokine receptors referred to as atypical chemokine receptors (ACKRs) are thought to non-signaling decoys because of their inability to activate typical G-protein signaling pathways. CXCR7, also known as ACKR3, binds to only two chemokines, SDF-1α and I-TAC, and recruits β-arrestins. SDF-1α also binds to its own conventional receptor, CXCR4, involving in homeostatic modulation such as development and immune surveillance as well as pathological conditions such as inflammation, ischemia, and cancers. Recently, CXCR7 is suggested as a key therapeutic target together with CXCR4 in such conditions. However, the molecular mechanisms underlying cellular responses and functional relation with CXCR7 and CXCR4 have not been elucidated, despite massive studies. Therefore, we aimed to reveal the molecular networks of CXCR7 and CXCR4 and compare their effects on cell migration.

methodsBase on structural complementation assay using NanoBiT technology, we characterized the distinct mechanisms underlying β-arrestin2 recruitment by both CXCR4 and CXCR7. Crosslinking and immunoprecipitation were conducted to analyze complex formation of the receptors. Gene deletion using CRISPR and reconstitution of the receptors were applied to analysis of ligand-dependent ERK phosphorylation and cell migration. All experiments were performed in triplicate and repeated more than three times. Unpaired Student's t-tests or ANOVA using PRISM5 software were employed for statistical analyses.

resultsLigand binding to CXCR7 does not result in activation of typical signaling pathways via Gα subunits but activation of GRK2 via βγ subunits and receptor phosphorylation with subsequent β-arrestin2 recruitment. In contrast, CXCR4 induced Gα

conclusionThis study demonstrates that SDF-1α-stimulated CXCR7 mediates β-arrestin2 recruitment via different molecular networking from that of CXCR4. CXCR7 may be neither a simple scavenger nor auxiliary receptor but plays an essential role in cell migration through cooperation with CXCR4.

Indexed as

Biased GPCRChemotaxisCXCR4CXCR7SDF-1αStructural complementation assay

Identifiers

PMID33292475
PMCPMC7686738
OpenAlexW3107666328

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.