Evidence map›Paper›PMID 32108028›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Tetraspanin-6 negatively regulates exosome production.

Rania Ghossoub, Marion Chéry, Stéphane Audebert, Raphael Leblanc, Antonio Luis Egea-Jimenez, Frédérique Lembo, Sarah Mammar, Flavien Le Dez, Luc Camoin, Jean-Paul Borg and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
4.4field-weighted citation impact, top 4% 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

65 citing papers in PubMed, 91 citations in OpenAlex.

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5 more citing papers are in PubMed but not listed here.

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

13 authors at 1 institution in 2 countries.

Rania GhossoubTeam Spatio-Temporal Regulation of Cell Signaling-Scaffolds & Phosphoinositides, Equipe Labellisée Ligue 2018, Centre de Recherche en Cancérologie de Marseille (CRCM), Institut Paoli-Calmettes, Aix-Marseille Université, Inserm, CNRS, 13009 Marseille, France.
Marion ChéryTeam Spatio-Temporal Regulation of Cell Signaling-Scaffolds & Phosphoinositides, Equipe Labellisée Ligue 2018, Centre de Recherche en Cancérologie de Marseille (CRCM), Institut Paoli-Calmettes, Aix-Marseille Université, Inserm, CNRS, 13009 Marseille, France.
Stéphane AudebertMarseille Proteomics Platform, CRCM, Institut Paoli-Calmettes, Aix-Marseille Université, Inserm, CNRS, 13009 Marseille, France.ORCID 0000-0002-9409-2588
Raphael LeblancTeam Spatio-Temporal Regulation of Cell Signaling-Scaffolds & Phosphoinositides, Equipe Labellisée Ligue 2018, Centre de Recherche en Cancérologie de Marseille (CRCM), Institut Paoli-Calmettes, Aix-Marseille Université, Inserm, CNRS, 13009 Marseille, France.
Antonio Luis Egea-JimenezTeam Spatio-Temporal Regulation of Cell Signaling-Scaffolds & Phosphoinositides, Equipe Labellisée Ligue 2018, Centre de Recherche en Cancérologie de Marseille (CRCM), Institut Paoli-Calmettes, Aix-Marseille Université, Inserm, CNRS, 13009 Marseille, France.ORCID 0000-0003-1684-2598
Frédérique LemboTeam Spatio-Temporal Regulation of Cell Signaling-Scaffolds & Phosphoinositides, Equipe Labellisée Ligue 2018, Centre de Recherche en Cancérologie de Marseille (CRCM), Institut Paoli-Calmettes, Aix-Marseille Université, Inserm, CNRS, 13009 Marseille, France.
Sarah MammarTeam Spatio-Temporal Regulation of Cell Signaling-Scaffolds & Phosphoinositides, Equipe Labellisée Ligue 2018, Centre de Recherche en Cancérologie de Marseille (CRCM), Institut Paoli-Calmettes, Aix-Marseille Université, Inserm, CNRS, 13009 Marseille, France.
Flavien Le DezTeam Spatio-Temporal Regulation of Cell Signaling-Scaffolds & Phosphoinositides, Equipe Labellisée Ligue 2018, Centre de Recherche en Cancérologie de Marseille (CRCM), Institut Paoli-Calmettes, Aix-Marseille Université, Inserm, CNRS, 13009 Marseille, France.
Luc CamoinMarseille Proteomics Platform, CRCM, Institut Paoli-Calmettes, Aix-Marseille Université, Inserm, CNRS, 13009 Marseille, France.
Jean-Paul BorgMarseille Proteomics Platform, CRCM, Institut Paoli-Calmettes, Aix-Marseille Université, Inserm, CNRS, 13009 Marseille, France.
Eric RubinsteinCentre d'Immunologie et des Maladies Infectieuses (CIMI)-Paris, Sorbonne Université, Inserm, CNRS, 75013 Paris, France.
Guido DavidTeam Spatio-Temporal Regulation of Cell Signaling-Scaffolds & Phosphoinositides, Equipe Labellisée Ligue 2018, Centre de Recherche en Cancérologie de Marseille (CRCM), Institut Paoli-Calmettes, Aix-Marseille Université, Inserm, CNRS, 13009 Marseille, France.
Pascale ZimmermannTeam Spatio-Temporal Regulation of Cell Signaling-Scaffolds & Phosphoinositides, Equipe Labellisée Ligue 2018, Centre de Recherche en Cancérologie de Marseille (CRCM), Institut Paoli-Calmettes, Aix-Marseille Université, Inserm, CNRS, 13009 Marseille, France; pascale.zimmermann@kuleuven.be.
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Exosomes, extracellular vesicles (EVs) of endosomal origin, emerge as master regulators of cell-to-cell signaling in physiology and disease. Exosomes are highly enriched in tetraspanins (TSPNs) and syndecans (SDCs), the latter occurring mainly in proteolytically cleaved form, as membrane-spanning C-terminal fragments of the proteins. While both protein families are membrane scaffolds appreciated for their role in exosome formation, composition, and activity, we currently ignore whether these work together to control exosome biology. Here we show that TSPN6, a poorly characterized tetraspanin, acts as a negative regulator of exosome release, supporting the lysosomal degradation of SDC4 and syntenin. We demonstrate that TSPN6 tightly associates with SDC4, the SDC4-TSPN6 association dictating the association of TSPN6 with syntenin and the TSPN6-dependent lysosomal degradation of SDC4-syntenin. TSPN6 also inhibits the shedding of the SDC4 ectodomain, mimicking the effects of matrix metalloproteinase inhibitors. Taken together, our data identify TSPN6 as a regulator of the trafficking and processing of SDC4 and highlight an important physical and functional interconnection between these membrane scaffolds for the production of exosomes. These findings clarify our understanding of the molecular determinants governing EV formation and have potentially broad impact for EV-related biomedicine.

Indexed as

Cell CommunicationExosomesExtracellular VesiclesHumansLysosomesMatrix MetalloproteinasesMCF-7 CellsProtein TransportSyndecan-4SyndecansSynteninsTetraspaninsMatrix MetalloproteinasesSDC4 protein, humanSyndecan-4SyndecansSynteninsTetraspaninsTSPAN32 protein, humanTSPAN6 protein, humanexosomessyndecansyntenintetraspanin

Identifiers

PMID32108028
PMCPMC7084133
OpenAlexW3008656969

What Socratic 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 Socratic graph.