Evidence map›Paper›PMID 26246139›Full record

ArticleJournal of immunology (Baltimore, Md. : 1950)2015

Ubiquitination as a Mechanism To Transport Soluble Mycobacterial and Eukaryotic Proteins to Exosomes.

Victoria L Smith, Liam Jackson, Jeffrey S Schorey

Open access · bronzeAbstract read
In one paragraph

Article in Journal of immunology (Baltimore, Md. : 1950), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

47 citing papers in PubMed, 79 citations in OpenAlex.

  1. Review
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  5. Article
  6. Structure and Functions of HMGB3 Protein.International journal of molecular sciences · 2024
    Review
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  10. Significance of extracellular vesicles in orchestration of immune responses inFrontiers in cellular and infection microbiology · 2024
    Review
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  15. Review
  16. Article
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  19. Extracellular Vesicles in Mycobacteria and Tuberculosis.Frontiers in cellular and infection microbiology · 2022
    Review
  20. Review
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

3 authors at 1 institution in 1 country.

Victoria L SmithDepartment of Biological Sciences, Eck Institute for Global Health, University of Notre Dame, Notre Dame, IN 46556.
Liam JacksonDepartment of Biological Sciences, Eck Institute for Global Health, University of Notre Dame, Notre Dame, IN 46556.
Jeffrey S SchoreyDepartment of Biological Sciences, Eck Institute for Global Health, University of Notre Dame, Notre Dame, IN 46556 schorey.1@nd.edu.
University of Notre Dame · US

Funding

M. avium GPLs in Macrophage Activation and VirulenceR01AI052439 · NIAID · UNIVERSITY OF NOTRE DAME · PI SCHOREY, JEFFREY SCOTT · 2004 to 2014
$3.4M
NIAID NIH HHS AI052439NIAID NIH HHS R01 AI052439
6 · The paper itself

Abstract

Exosomes are extracellular vesicles of endocytic origin that function in intercellular communication. Our previous studies indicate that exosomes released from Mycobacterium tuberculosis-infected macrophages contain soluble mycobacterial proteins. However, it was unclear how these secreted proteins were targeted to exosomes. In this study, we determined that exosome production by the murine macrophage cell line RAW264.7 requires the endosomal sorting complexes required for transport and that trafficking of mycobacterial proteins from phagocytosed bacilli to exosomes was dependent on protein ubiquitination. Moreover, soluble mycobacterial proteins, when added exogenously to RAW264.7 or human HEK293 cells, were endocytosed, ubiquitinated, and released via exosomes. This suggested that endocytosed proteins could be recycled from cells through exosomes. This hypothesis was supported using the tumor-associated protein He4, which, when endocytosed by RAW264.7 or HEK293 cells, was transported to exosomes in a ubiquitin-dependent manner. Our data suggest that ubiquitination is a modification sufficient for trafficking soluble proteins within the phagocytic/endocytic network to exosomes.

Indexed as

AnimalsAntigens, BacterialBacterial ProteinsCell CommunicationCell LineClathrinDNA-Binding ProteinsEndocytosisEndosomal Sorting Complexes Required for TransportExosomesHeat-Shock ProteinsHEK293 CellsHumansMacrophagesMiceMycobacterium smegmatisAntigens, BacterialBacterial ProteinsClathrinDNA-Binding ProteinsEndosomal Sorting Complexes Required for TransportgroES protein, Mycobacterium tuberculosisHeat-Shock Proteinshepatocyte growth factor-regulated tyrosine kinase substrateHspX protein, Mycobacterium tuberculosisparkin proteinPhosphoproteinsProteinsRNA, Small InterferingTranscription FactorsTsg101 ProteinUbiquitin-Protein LigasesWAP Four-Disulfide Core Domain Protein 2Wfdc2 protein, mouse

Identifiers

PMID26246139
PMCPMC5706551
OpenAlexW1937096559

What OpenQuestion holds

Textmetadata
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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.