Evidence map›Paper›PMID 25261472›Full record

ArticleThe Journal of biological chemistry2014

Complex N-linked glycans serve as a determinant for exosome/microvesicle cargo recruitment.

Yaxuan Liang, William S Eng, David R Colquhoun, Rhoel R Dinglasan, David R Graham, Lara K Mahal

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

78 citing papers in PubMed, 150 citations in OpenAlex.

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  14. Exosome Mediated Cell-Cell Crosstalk in Tissue Injury and Repair.Results and problems in cell differentiation · 2024
    Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Exploiting the biogenesis of extracellular vesicles for bioengineering and therapeutic cargo loading.Molecular therapy : the journal of the American Society of Gene Therapy · 2023
    Review

18 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

6 authors at 2 institutions in 1 country.

Yaxuan LiangFrom the Biomedical Chemistry Institute, Department of Chemistry, New York University, New York, New York 10003-6688.
William S EngFrom the Biomedical Chemistry Institute, Department of Chemistry, New York University, New York, New York 10003-6688.
David R ColquhounDepartment of Molecular and Comparative Pathobiology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, and.
Rhoel R DinglasanW. Harry Feistone Department of Molecular Microbiology and Immunology, Johns Hopkins Bloomberg School of Public Health, Baltimore, Maryland 21205.
David R GrahamDepartment of Molecular and Comparative Pathobiology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, and.
Lara K MahalFrom the Biomedical Chemistry Institute, Department of Chemistry, New York University, New York, New York 10003-6688, lkmahal@nyu.edu.
Johns Hopkins University · USNew York University · US

Funding

An integrated systems approach to deconstructing glycosylationDP2OD004711 · OD · UNIVERSITY OF TEXAS AT AUSTIN · PI MAHAL, LARA K. · 2008 to 2008
$1.8M
NIH HHS 7 DP2 OD004711-02NIH HHS DP2 OD004711
6 · The paper itself

Abstract

Exosomes, also known as microvesicles (EMVs), are nano-sized membranous particles secreted from nearly all mammalian cell types. These nanoparticles play critical roles in many physiological processes including cell-cell signaling, immune activation, and suppression and are associated with disease states such as tumor progression. The biological functions of EMVs are highly dependent on their protein composition, which can dictate pathogenicity. Although some mechanisms have been proposed for the regulation of EMV protein trafficking, little attention has been paid to N-linked glycosylation as a potential sorting signal. Previous work from our laboratory found a conserved glycan signature for EMVs, which differed from that of the parent cell membranes, suggesting a potential role for glycosylation in EMV biogenesis. In this study, we further explore the role of glycosylation in EMV protein trafficking. We identify EMV glycoproteins and demonstrate alteration of their recruitment as a function of their glycosylation status upon pharmacological manipulation. Furthermore, we show that genetic manipulation of the glycosylation levels of a specific EMV glycoprotein, EWI-2, directly impacts its recruitment as a function of N-linked glycan sites. Taken together, our data provide strong evidence that N-linked glycosylation directs glycoprotein sorting into EMVs.

Indexed as

Antigens, CDBlotting, WesternCell Line, TumorCell MembraneExosomesGlycoproteinsGlycosylationHumansMembrane ProteinsMicroscopy, FluorescencePolysaccharidesProtein TransportRNA InterferenceTetraspanin 28Tetraspanin 30Antigens, CDGlycoproteinsIGSF8 protein, humanMembrane ProteinsPolysaccharidesTetraspanin 28Tetraspanin 30Carbohydrate FunctionExosomeG3BPGalectinGlycosylationIgFS8Intracellular TraffickingMembrane TraffickingMicrovesicleTetraspanin

Identifiers

PMID25261472
PMCPMC4239607
OpenAlexW2091618419

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.