Evidence map›Paper›PMID 17475775›Full record

ArticleMolecular biology of the cell2007

The role of Trs65 in the Ypt/Rab guanine nucleotide exchange factor function of the TRAPP II complex.

Yongheng Liang, Nadya Morozova, Andrei A Tokarev, Jonathan W Mulholland, Nava Segev

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

29 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Structural basis for Rab6 activation by the Ric1-Rgp1 complex.bioRxiv : the preprint server for biology · 2024
    Article
  5. Vtc4 Promotes the Entry of Phagophores into Vacuoles in theJournal of fungi (Basel, Switzerland) · 2023
    Article
  6. Article
  7. Article
  8. Article
  9. Arf1 orchestrates Rab GTPase conversion at theMolecular biology of the cell · 2021
    Article
  10. Article
  11. Article
  12. Review
  13. Rab5-dependent autophagosome closure by ESCRT.The Journal of cell biology · 2019
    Article
  14. Article
  15. Article
  16. Article
  17. TRAPP Complexes in Secretion and Autophagy.Frontiers in cell and developmental biology · 2016
    Review
  18. Ypt/Rab GTPases: principles learned from yeast.Critical reviews in biochemistry and molecular biology · 2015
    Review
  19. A Vps21 endocytic module regulates autophagy.Molecular biology of the cell · 2014
    Article
  20. 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

5 authors at 2 institutions in 1 country.

Yongheng LiangDepartment of Biological Sciences, Laboratory for Molecular Biology, University of Illinois, Chicago, IL 60607, USA.
Nadya Morozova
Andrei A Tokarev
Jonathan W Mulholland
Nava Segev
University of Illinois Chicago · USStanford University · US

Funding

YPTL GTPASE AND VESICULAR TRANSPORTR01GM045444 · NIGMS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI SEGEV, NAVA · 1992 to 2020
$6.4M
NIGMS NIH HHS GM-45444NIGMS NIH HHS R01 GM045444
6 · The paper itself

Abstract

The conserved modular complex TRAPP is a guanine nucleotide exchanger (GEF) for the yeast Golgi Ypt-GTPase gatekeepers. TRAPP I and TRAPP II share seven subunits and act as GEFs for Ypt1 and Ypt31/32, respectively, which in turn regulate transport into and out of the Golgi. Trs65/Kre11 is one of three TRAPP II-specific subunits. Unlike the other two subunits, Trs120 and Trs130, Trs65 is not essential for viability, is conserved only among some fungi, and its contribution to TRAPP II function is unclear. Here, we provide genetic, biochemical, and cellular evidence for the role of Trs65 in TRAPP II function. First, like Trs130, Trs65 localizes to the trans-Golgi. Second, TRS65 interacts genetically with TRS120 and TRS130. Third, Trs65 interacts physically with Trs120 and Trs130. Finally, trs65 mutant cells have low levels of Trs130 protein, and they are defective in the GEF activity of TRAPP II and the intracellular distribution of Ypt1 and Ypt31/32. Together, these results show that Trs65 plays a role in the Ypt GEF activity of TRAPP II in concert with the two other TRAPP II-specific subunits. Elucidation of the role played by Trs65 in intracellular trafficking is important for understanding how this process is coordinated with two other processes in which Trs65 is implicated: cell wall biogenesis and stress response.

Indexed as

Golgi ApparatusGuanine Nucleotide Exchange FactorsMembrane ProteinsModels, BiologicalMutationPhenotypeProtein BindingProtein SubunitsProtein Transportrab GTP-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsGuanine Nucleotide Exchange FactorsMembrane ProteinsProtein Subunitsrab GTP-Binding ProteinsSaccharomyces cerevisiae Proteinstransport protein particle, TRAPPTRS65 protein, S cerevisiaeVesicular Transport ProteinsYPT1 protein, S cerevisiae

Identifiers

PMID17475775
PMCPMC1924837
OpenAlexW2137921838

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.