Evidence map›Paper›PMID 21813735›Full record

ArticleMolecular biology of the cell2011

Trs65p, a subunit of the Ypt1p GEF TRAPPII, interacts with the Arf1p exchange factor Gea2p to facilitate COPI-mediated vesicle traffic.

Shuliang Chen, Huaqing Cai, Sei-Kyoung Park, Shekar Menon, Catherine L Jackson, Susan Ferro-Novick

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

20 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
  2. Sec7 regulatory domains scaffold autoinhibited and active conformations.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. Review
  4. The p24 Complex Contributes to Specify Arf1 for COPI Coat Selection.International journal of molecular sciences · 2021
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. TRAPP Complexes in Secretion and Autophagy.Frontiers in cell and developmental biology · 2016
    Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. Review
  17. Ypt1 recruits the Atg1 kinase to the preautophagosomal structure.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  18. A trapper keeper for TRAPP, its structures and functions.Cellular and molecular life sciences : CMLS · 2012
    Review
  19. GEF-effector interactions.Cellular logistics
    Article
  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

6 authors at 2 institutions in 1 country.

Shuliang ChenDepartment of Cellular and Molecular Medicine, Howard Hughes Medical Institute, University of California at San Diego, La Jolla, CA 92093-0668, USA.
Huaqing Cai
Sei-Kyoung Park
Shekar Menon
Catherine L Jackson
Susan Ferro-Novick
Howard Hughes Medical Institute · USEunice Kennedy Shriver National Institute of Child Health and Human Development · US

Funding

Howard Hughes Medical InstituteIntramural NIH HHS
6 · The paper itself

Abstract

The TRAPP complexes are multimeric guanine exchange factors (GEFs) for the Rab GTPase Ypt1p. The three complexes (TRAPPI, TRAPPII, and TRAPPIII) share a core of common subunits required for GEF activity, as well as unique subunits (Trs130p, Trs120p, Trs85p, and Trs65p) that redirect the GEF from the endoplasmic reticulum-Golgi pathway to different cellular locations where TRAPP mediates distinct membrane trafficking events. Roles for three of the four unique TRAPP subunits have been described before; however, the role of the TRAPPII-specific subunit Trs65p has remained elusive. Here we demonstrate that Trs65p directly binds to the C-terminus of the Arf1p exchange factor Gea2p and provide in vivo evidence that this interaction is physiologically relevant. Gea2p and TRAPPII also bind to the yeast orthologue of the γ subunit of the COPI coat complex (Sec21p), a known Arf1p effector. These and previous findings reveal that TRAPPII is part of an Arf1p GEF-effector loop that appears to play a role in recruiting or stabilizing TRAPPII to membranes. In support of this proposal, we show that TRAPPII is more soluble in an arf1Δ mutant.

Indexed as

ADP-Ribosylation Factor 1Chloride ChannelsCOP-Coated VesiclesEndoplasmic ReticulumGene Expression Regulation, FungalGolgi ApparatusGuanine Nucleotide Exchange FactorsProtein BindingProtein Transportrab GTP-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSolubilityVesicular Transport ProteinsADP-Ribosylation Factor 1Chloride ChannelsGEA2 protein, S cerevisiaeGEF1 protein, S cerevisiaeGuanine Nucleotide Exchange Factorsrab GTP-Binding ProteinsSaccharomyces cerevisiae Proteinstransport protein particle, TRAPPTRS65 protein, S cerevisiaeVesicular Transport ProteinsYPT1 protein, S cerevisiae

Identifiers

PMID21813735
PMCPMC3183018
OpenAlexW2090145593

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.