Evidence map›Paper›PMID 28331048›Full record

ArticleMolecular pharmacology2017

G Protein-Coupled Receptor Kinase 3 and Protein Kinase C Phosphorylate the Distal C-Terminal Tail of the Chemokine Receptor CXCR4 and Mediate Recruitment of

Jiansong Luo, John M Busillo, Ralf Stumm, Jeffrey L Benovic

Open access · bronzeAbstract read
In one paragraph

Article in Molecular pharmacology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

26 citing papers in PubMed, 41 citations in OpenAlex.

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  8. Crosstalk between CXCR4/ACKR3 and EGFR Signaling in Breast Cancer Cells.International journal of molecular sciences · 2022
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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

4 authors at 1 institution in 2 countries.

Jiansong LuoDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, Pennsylvania (J.L., J.M.B., J.L.B.); and Institute of Pharmacology and Toxicology, University Hospital, Friedrich-Schiller University, Jena, Germany (R.S.).
John M BusilloDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, Pennsylvania (J.L., J.M.B., J.L.B.); and Institute of Pharmacology and Toxicology, University Hospital, Friedrich-Schiller University, Jena, Germany (R.S.).
Ralf StummDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, Pennsylvania (J.L., J.M.B., J.L.B.); and Institute of Pharmacology and Toxicology, University Hospital, Friedrich-Schiller University, Jena, Germany (R.S.).
Jeffrey L BenovicDepartment of Biochemistry and Molecular Biology, Thomas Jefferson University, Philadelphia, Pennsylvania (J.L., J.M.B., J.L.B.); and Institute of Pharmacology and Toxicology, University Hospital, Friedrich-Schiller University, Jena, Germany (R.S.) jeffrey.benovic@jefferson.edu.
Friedrich Schiller University Jena · DE

Funding

X-Ray Crystallography and Macromolecular CharacterizationP30CA056036 · NCI · THOMAS JEFFERSON UNIVERSITY · PI DANIEL P SILVER · 1995 to 2026
$94.8M
G PROTEIN-COUPLED RECEPTOR KINASESR01GM044944 · NIGMS · THOMAS JEFFERSON UNIVERSITY · PI BENOVIC, JEFFREY L · 1990 to 2016
$5.3M
Role of Arrestins in G Protein-Coupled Receptor RegulationR37GM047417 · NIGMS · THOMAS JEFFERSON UNIVERSITY · PI BENOVIC, JEFFREY L · 2006 to 2015
$4.3M
Regulation of CXCR4 SignalingR01CA129626 · NCI · THOMAS JEFFERSON UNIVERSITY · PI BENOVIC, JEFFREY L · 2007 to 2011
$1.5M
NCI NIH HHS P30 CA056036NCI NIH HHS R01 CA129626NIGMS NIH HHS R01 GM044944NIGMS NIH HHS R37 GM047417
6 · The paper itself

Abstract

Phosphorylation of G protein-coupled receptors (GPCRs) is a key event for cell signaling and regulation of receptor function. Previously, using tandem mass spectrometry, we identified two phosphorylation sites at the distal C-terminal tail of the chemokine receptor CXCR4, but were unable to determine which specific residues were phosphorylated. Here, we demonstrate that serines (Ser) 346 and/or 347 (Ser-346/7) of CXCR4 are phosphorylated upon stimulation with the agonist CXCL12 as well as a CXCR4 pepducin, ATI-2341. ATI-2341, a G

Indexed as

beta-ArrestinsG-Protein-Coupled Receptor Kinase 3HEK293 CellsHumansIsoenzymesPhosphorylationProtein Kinase CProtein Kinase InhibitorsReceptors, CXCR4Serinebeta-ArrestinsCXCR4 protein, humanG-Protein-Coupled Receptor Kinase 3GRK3 protein, humanIsoenzymesProtein Kinase CProtein Kinase InhibitorsReceptors, CXCR4Serine

Identifiers

PMID28331048
PMCPMC5438129
OpenAlexW2597463553

What OpenQuestion holds

Textmetadata
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.