Evidence map›Paper›PMID 18694437›Full record

ArticleTraffic (Copenhagen, Denmark)2008

Arabidopsis has two functional orthologs of the yeast V-ATPase assembly factor Vma21p.

Christoph Neubert, Laurie A Graham, Eric W Black-Maier, Emily M Coonrod, Tzu-Yin Liu, York-Dieter Stierhof, Thorsten Seidel, Tom H Stevens, Karin Schumacher

Open access · bronzeAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

12 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Review
  3. Detection of Stress-Induced Changes in Subcellular Protein Distribution.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  4. Review
  5. The Plant V-ATPase.Frontiers in plant science · 2022
    Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. 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

9 authors at 4 institutions in 2 countries.

Christoph NeubertCenter for Plant Molecular Biology, ZMBP, University of Tübingen, Auf der Morgenstelle 1, 72076 Tübingen, Germany.
Laurie A Graham
Eric W Black-Maier
Emily M Coonrod
Tzu-Yin Liu
York-Dieter Stierhof
Thorsten Seidel
Tom H Stevens
Karin Schumacher
University of Oregon · USUniversity of Tübingen · DEBielefeld University · DEHeidelberg University · DE

Funding

SORTING AND TRANSPORT OF YEAST MEMBRANE PROTEINSR01GM038006 · NIGMS · UNIVERSITY OF OREGON · PI STEVENS, TOM HALL · 1987 to 2016
$4.9M
The role of the endocytic pathway in glucose sensing in S. cerevisiaeF32GM083572 · NIGMS · UNIVERSITY OF OREGON · PI COONROD, EMILY · 2008 to 2009
$97k
NIGMS NIH HHS 1F32GM083572-01NIGMS NIH HHS F32 GM083572NIGMS NIH HHS GM38006NIGMS NIH HHS R01 GM038006
6 · The paper itself

Abstract

How individual protein subunits assemble into the higher order structure of a protein complex is not well understood. Four proteins dedicated to the assembly of the V(0) subcomplex of the V-adenosine triphosphatase (V-ATPase) in the endoplasmic reticulum (ER) have been identified in yeast, but their precise mode of molecular action remains to be identified. In contrast to the highly conserved subunits of the V-ATPase, orthologs of the yeast assembly factors are not easily identified based on sequence similarity. We show in this study that two ER-localized Arabidopsis proteins that share only 25% sequence identity with Vma21p can functionally replace this yeast assembly factor. Loss of AtVMA21a function in RNA interference seedlings caused impaired cell expansion and changes in Golgi morphology characteristic for plants with reduced V-ATPase activity, and we therefore conclude that AtVMA21a is the first V-ATPase assembly factor identified in a multicellular eukaryote. Moreover, VMA21p acts as a dedicated ER escort chaperone, a class of substrate-specific accessory proteins so far not identified in higher plants.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsChaperoninsElectrophoresis, Polyacrylamide GelEndoplasmic ReticulumGolgi ApparatusGreen Fluorescent ProteinsMembrane ProteinsMicroscopy, ImmunoelectronMolecular Sequence DataPlasmidsProtein SubunitsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidArabidopsis ProteinsAtVMA21a protein, ArabidopsisAtVMA21b protein, ArabidopsisChaperoninsGreen Fluorescent ProteinsMembrane ProteinsProtein SubunitsSaccharomyces cerevisiae ProteinsVacuolar Proton-Translocating ATPasesVMA21 protein, S cerevisiae

Identifiers

PMID18694437
PMCPMC2953365
OpenAlexW2003505606

What OpenQuestion holds

Textmetadata
LicenceTDM
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.