Evidence map›Paper›PMID 25750764›Full record

ArticleCellular logistics

The Vps39-like TRAP1 is an effector of Rab5 and likely the missing Vps3 subunit of human CORVET.

Jens Lachmann, Elina Glaubke, Patrick S Moore, Christian Ungermann

Open access · bronzeAbstract read
In one paragraph

Article in Cellular logistics. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

19 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. TbVps41 regulates trafficking of endocytic but not biosynthetic cargo to lysosomes of bloodstream forms of Trypanosoma brucei.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  4. Mucopolysaccharidosis-Plus Syndrome.International journal of molecular sciences · 2020
    Article
  5. Article
  6. Article
  7. The lysosomal disease caused by mutant VPS33A.Human molecular genetics · 2019
    Article
  8. Article
  9. Article
  10. Review
  11. Distinct sets of tethering complexes, SNARE complexes, and Rab GTPases mediate membrane fusion at the vacuole in Arabidopsis.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
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

4 authors at 2 institutions in 2 countries.

Jens LachmannDepartment of Biology/Chemistry; Biochemistry Section; University of Osnabruck ; Osnabrück, Germany .
Elina GlaubkeDepartment of Biology/Chemistry; Biochemistry Section; University of Osnabruck ; Osnabrück, Germany .
Patrick S MooreUniversity of Pittsburgh Cancer Institute; Cancer Virology Program ; Pittsburgh, PA USA .
Christian UngermannDepartment of Biology/Chemistry; Biochemistry Section; University of Osnabruck ; Osnabrück, Germany .
Osnabrück University · DEUniversity of Pittsburgh · US

Funding

Protein Biomarkers for a New Human Polyomavirus in AIDS-related MalignanciesR01CA136363 · NCI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI MOORE, PATRICK S. · 2008 to 2015
$2.3M
NCI NIH HHS R01 CA136363
6 · The paper itself

Abstract

Membrane fusion in the endocytic pathway is mediated by a protein machinery consistent of Rab GTPases, tethering factors and SNAREs. In yeast, the endosomal CORVET and lysosomal HOPS tethering complexes share 4 of their 6 subunits. The 2 additional subunits in each complex - Vps3 and Vps8 for CORVET, and the homologous Vps39 and Vps41 for HOPS - bind directly to Rab5 and Rab7, respectively. In humans, all subunits for HOPS have been described. However, human CORVET remains poorly characterized and a homolog of Vps3 is still missing. Here we characterize 2 previously identified Vps39 isoforms, hVps39-1/hVam6/TLP and hVps39-2/TRAP1, in yeast and HEK293 cells. None of them can compensate the loss of the endogenous yeast Vps39, though the specific interaction of hVps39-1 with the virus-specific LT protein was reproduced. Both human Vps39 proteins show a cytosolic localization in yeast and mammalian cells. However, hVps39-2/TRAP1 strongly co-localizes with co-expressed Rab5 and interacts directly with Rab5-GTP in vitro. We conclude that hVps39-2/TRAP1 is an endosomal protein and an effector of Rab5, suggesting a role of the protein as a subunit of the putative human CORVET complex.

Indexed as

CORVETfusionHOPSMembrane tetheringRab GTPasesTRAP1Vps39

Identifiers

PMID25750764
PMCPMC4325178
OpenAlexW1981606711

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.