Evidence map›Paper›PMID 30018135›Full record

ArticleThe Journal of biological chemistry2018

VAMP-associated protein-A and oxysterol-binding protein-related protein 3 promote the entry of late endosomes into the nucleoplasmic reticulum.

Mark F Santos, Germana Rappa, Jana Karbanová, Thomas Kurth, Denis Corbeil, Aurelio Lorico

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
–field-weighted citation impact
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

50 citing papers in PubMed.

  1. Article
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  4. Review
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  9. Mechanisms for assembly of the nucleoplasmic reticulum.Cellular and molecular life sciences : CMLS · 2024
    Review
  10. Review
  11. Article
  12. Article
  13. Review
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  15. Verticillium longisporum phospholipase VlsPLAMolecular plant pathology · 2023
    Article
  16. Article
  17. Review
  18. Article
  19. 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.

Mark F SantosFrom the Roseman Cancer Center and Department of Pathology, Roseman University College of Medicine, Las Vegas, Nevada 89135.
Germana RappaFrom the Roseman Cancer Center and Department of Pathology, Roseman University College of Medicine, Las Vegas, Nevada 89135.
Jana Karbanováthe Biotechnology Center and.
Thomas Kurththe Biotechnology Center and.
Denis CorbeilFrom the Roseman Cancer Center and Department of Pathology, Roseman University College of Medicine, Las Vegas, Nevada 89135, denis.corbeil@tu-dresden.de.
Aurelio LoricoFrom the Roseman Cancer Center and Department of Pathology, Roseman University College of Medicine, Las Vegas, Nevada 89135, alorico@roseman.edu aurelio.lorico@fondazioneiom.it.ORCID 0000-0003-0644-7375

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The endocytic pathway plays an instrumental role in recycling internalized molecules back to the plasma membrane or in directing them to lysosomes for degradation. We recently reported a new role of endosomes-the delivery of components from extracellular vesicles (EVs) to the nucleoplasm of recipient cells. Using indirect immunofluorescence, FRET, immunoisolation techniques, and RNAi, we report here a tripartite protein complex (referred to as the VOR complex) that is essential for the nuclear transfer of EV-derived components by orchestrating the specific localization of late endosomes into nucleoplasmic reticulum. We found that the VOR complex contains the endoplasmic reticulum-localized vesicle-associated membrane protein (VAMP)-associated protein A (VAP-A), the cytoplasmic oxysterol-binding protein-related protein 3 (ORP3), and late endosome-associated small GTPase Rab7. The silencing of VAP-A or ORP3 abrogated the association of Rab7-positive late endosomes with nuclear envelope invaginations and, hence, the transport of endocytosed EV-derived components to the nucleoplasm of recipient cells. We conclude that the VOR complex can be targeted to inhibit EV-mediated intercellular communication, which can have therapeutic potential for managing cancer in which the release of EVs is dysregulated.

Indexed as

Carrier ProteinsCell CommunicationCells, CulturedEndocytosisEndoplasmic ReticulumEndosomesFatty Acid-Binding ProteinsHumansMultiprotein ComplexesNuclear EnvelopeOxysterol Binding Proteinsrab7 GTP-Binding Proteinsrab GTP-Binding ProteinsReceptors, SteroidR-SNARE ProteinsVesicular Transport ProteinsCarrier ProteinsFatty Acid-Binding ProteinsMultiprotein ComplexesOSBPL3 protein, humanOxysterol Binding Proteinsrab7 GTP-Binding Proteinsrab7 GTP-binding proteins, humanrab GTP-Binding ProteinsReceptors, SteroidR-SNARE ProteinsVAPA protein, humanVesicular Transport Proteinscancer biologyendocytosisendosomeexosome (vesicle)extracellular vesicleslate endosomenuclear envelopenuclear transportnucleusORP3oxysterol-binding related proteinVAP-Avesicle-associated membrane protein;VOR complex

Identifiers

PMID30018135
PMCPMC6130944

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.