Evidence map›Paper›PMID 25759509›Full record

ArticleMolecular & cellular proteomics : MCP2015

A Fluorescent Live Imaging Screening Assay Based on Translocation Criteria Identifies Novel Cytoplasmic Proteins Implicated in G Protein-coupled Receptor Signaling Pathways.

Sandra Lecat, Hans W D Matthes, Rainer Pepperkok, Jeremy C Simpson, Jean-Luc Galzi

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

15 citing papers in PubMed, 24 citations in OpenAlex.

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  9. CLIC4/Arf6 Pathway.Circulation research · 2019
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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

5 authors at 4 institutions in 3 countries.

Sandra LecatFrom the ‡GPCRs, Pain and Inflammation Team, UMR7242, CNRS-University of Strasbourg, LabEx Medalis, 300 Bvd Sébastien Brant, 67412 Illkirch, France; sandra.lecat@unistra.fr.
Hans W D MatthesFrom the ‡GPCRs, Pain and Inflammation Team, UMR7242, CNRS-University of Strasbourg, LabEx Medalis, 300 Bvd Sébastien Brant, 67412 Illkirch, France;
Rainer Pepperkok§European Molecular Biology Laboratory, Advanced Light Microscopy Facility, Meyerhofstr 1, 69117 Heidelberg, Germany;
Jeremy C Simpson¶¶School of Biology and Environmental Science and UCD Conway Institute, University College Dublin, Dublin 4, Ireland.
Jean-Luc GalziFrom the ‡GPCRs, Pain and Inflammation Team, UMR7242, CNRS-University of Strasbourg, LabEx Medalis, 300 Bvd Sébastien Brant, 67412 Illkirch, France;
Université de Strasbourg · FRBiotechnologie et Signalisation Cellulaire · FREuropean Molecular Biology Laboratory · DEUniversity College Dublin · IE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Several cytoplasmic proteins that are involved in G protein-coupled receptor signaling cascades are known to translocate to the plasma membrane upon receptor activation, such as beta-arrestin2. Based on this example and in order to identify new cytoplasmic proteins implicated in the ON-and-OFF cycle of G protein-coupled receptor, a live-imaging screen of fluorescently labeled cytoplasmic proteins was performed using translocation criteria. The screening of 193 fluorescently tagged human proteins identified eight proteins that responded to activation of the tachykinin NK2 receptor by a change in their intracellular localization. Previously we have presented the functional characterization of one of these proteins, REDD1, that translocates to the plasma membrane. Here we report the results of the entire screening. The process of cell activation was recorded on videos at different time points and all the videos can be visualized on a dedicated website. The proteins BAIAP3 and BIN1, partially translocated to the plasma membrane upon activation of NK2 receptors. Proteins ARHGAP12 and PKM2 translocated toward membrane blebs. Three proteins that associate with the cytoskeleton were of particular interest : PLEKHH2 rearranged from individual dots located near the cell-substrate adhesion surface into lines of dots. The speriolin-like protein, SPATC1L, redistributed to cell-cell junctions. The Chloride intracellular Channel protein, CLIC2, translocated from actin-enriched plasma membrane bundles to cell-cell junctions upon activation of NK2 receptors. CLIC2, and one of its close paralogs, CLIC4, were further shown to respond with the same translocation pattern to muscarinic M3 and lysophosphatidic LPA receptors. This screen allowed us to identify potential actors in signaling pathways downstream of G protein-coupled receptors and could be scaled-up for high-content screening.

Indexed as

Biological AssaySignal TransductionAdaptor Proteins, Signal TransducingBacterial ProteinsCarrier ProteinsChloride ChannelsCytoskeletal ProteinsGene Expression RegulationGenes, ReporterGreen Fluorescent ProteinsGTPase-Activating ProteinsHEK293 CellsHumansIntracellular Signaling Peptides and ProteinsLuminescent ProteinsMembrane ProteinsAdaptor Proteins, Signal TransducingARHGAP12 protein, humanBacterial ProteinsBAIAP3 protein, humanBIN1 protein, humanCarrier ProteinsChloride ChannelsCLIC2 protein, humanCLIC4 protein, humanCyan Fluorescent ProteinCytoskeletal ProteinsGreen Fluorescent ProteinsGTPase-Activating ProteinsIntracellular Signaling Peptides and ProteinsLuminescent ProteinsMembrane ProteinsNerve Tissue ProteinsNuclear Proteinsplekhh2 protein, humanReceptors, Neurokinin-2Recombinant ProteinsSPATC1 protein, humanThyroid Hormone-Binding ProteinsThyroid HormonesTumor Suppressor Proteinsyellow fluorescent protein, Bacteria

Identifiers

PMID25759509
PMCPMC4424407
OpenAlexW2143360793

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.