Evidence map›Paper›PMID 26884507›Full record

ArticleMolecular & cellular proteomics : MCP2016

Deubiquitylation of Protein Cargo Is Not an Essential Step in Exosome Formation.

Alyssa R Huebner, Lei Cheng, Poorichaya Somparn, Mark A Knepper, Robert A Fenton, Trairak Pisitkun

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
5.2field-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

36 citing papers in PubMed, 61 citations in OpenAlex.

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  12. Extracellular vesicles fromFrontiers in immunology · 2022
    Article
  13. The ClJournal of human hypertension · 2021
    Article
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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

6 authors at 3 institutions in 3 countries.

Alyssa R HuebnerFrom the ‡Department of Biomedicine and Center for Interactions of Proteins in Epithelial Transport, Aarhus University, Denmark;
Lei ChengFrom the ‡Department of Biomedicine and Center for Interactions of Proteins in Epithelial Transport, Aarhus University, Denmark;
Poorichaya Somparn§Faculty of Medicine, Chulalongkorn University, Bangkok, Thailand;
Mark A Knepper¶Epithelial Systems Biology Laboratory, NHLBI, National Institutes of Health, Bethesda, MD 20892-1603.
Robert A FentonFrom the ‡Department of Biomedicine and Center for Interactions of Proteins in Epithelial Transport, Aarhus University, Denmark; trairak@gmail.com robert.a.fenton@biomed.au.dk.
Trairak PisitkunFrom the ‡Department of Biomedicine and Center for Interactions of Proteins in Epithelial Transport, Aarhus University, Denmark; §Faculty of Medicine, Chulalongkorn University, Bangkok, Thailand; trairak@gmail.com robert.a.fenton@biomed.au.dk.
Aarhus University · DKChulalongkorn University · THNational Heart Lung and Blood Institute · US

Funding

Solute And Water Transport In Renal EpitheliaZIAHL001285 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI KNEPPER, MARK · 2009 to 2025
$34.9M
Computational Tools for ProteomicsZIAHL006129 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI KNEPPER, MARK · 2011 to 2025
$8.1M
Urinary ExosomesZIAHL006128 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI KNEPPER, MARK · 2011 to 2019
$354k
6 · The paper itself

Abstract

Exosomes, derived from multivesicular bodies (MVBs), contain proteins and genetic materials from their cell of origin and are secreted from various cells types, including kidney epithelial cells. In general, it is thought that protein cargo is ubiquitylated but that ubiquitin is cleaved by specific deubiquitylases during the process of cargo incorporation into MVBs. Here, we provide direct evidence that, in vivo, deubiquitylation is not essential. Ubiquitin was detected within human MVBs and urinary exosomes by electron microscopy. Of the >6000 proteins identified in human urinary exosomes was mass spectrometry, 15% were ubiquitylated with various topologies (Lys63>Lys48> Lys11>Lys6>Lys29>Lys33>Lys27). A significant preference for basic amino acids upstream of ubiquitylation sites suggests specific ubiquitylation motifs. The current studies demonstrate that, in vivo, deubiquitylation of proteins is not necessary for their incorporation into MVBs and highlight that urinary exosomes are an enriched source for studying ubiquitin modifications in physiological or disease states.

Indexed as

AdultAmino Acid MotifsEpithelial CellsExosomesHumansKidneyMass SpectrometryProteinsProteomicsUbiquitinationUbiquitinsUrineYoung AdultProteinsUbiquitins

Identifiers

PMID26884507
PMCPMC4858939
OpenAlexW2279242971

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.