Evidence map›Paper›PMID 21737673›Full record

ArticleMolecular biology of the cell2011

The reconstructed ancestral subunit a functions as both V-ATPase isoforms Vph1p and Stv1p in Saccharomyces cerevisiae.

Gregory C Finnigan, Victor Hanson-Smith, Benjamin D Houser, Hae J Park, Tom H Stevens

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 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

18 citing papers in PubMed, 26 citations in OpenAlex.

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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

5 authors at 1 institution in 1 country.

Gregory C FinniganInstitute of Molecular Biology, University of Oregon, Eugene, OR 97403, USA.
Victor Hanson-Smith
Benjamin D Houser
Hae J Park
Tom H Stevens
University of Oregon · US

Funding

SORTING AND TRANSPORT OF YEAST MEMBRANE PROTEINSR01GM038006 · NIGMS · UNIVERSITY OF OREGON · PI STEVENS, TOM HALL · 1987 to 2016
$4.9M
SYSTEMS PHYSIOLOGY TRAINING PROGRAMT32GM007257 · NIGMS · UNIVERSITY OF OREGON · PI LOCKERY, SHAWN R · 1985 to 2009
$1.6M
NIGMS NIH HHS GM38006NIGMS NIH HHS R01 GM038006NIGMS NIH HHS T32 GM007257
6 · The paper itself

Abstract

The vacuolar-type, proton-translocating ATPase (V-ATPase) is a multisubunit enzyme responsible for organelle acidification in eukaryotic cells. Many organisms have evolved V-ATPase subunit isoforms that allow for increased specialization of this critical enzyme. Differential targeting of the V-ATPase to specific subcellular organelles occurs in eukaryotes from humans to budding yeast. In Saccharomyces cerevisiae, the two subunit a isoforms are the only difference between the two V-ATPase populations. Incorporation of Vph1p or Stv1p into the V-ATPase dictates the localization of the V-ATPase to the vacuole or late Golgi/endosome, respectively. A duplication event within fungi gave rise to two subunit a genes. We used ancestral gene reconstruction to generate the most recent common ancestor of Vph1p and Stv1p (Anc.a) and tested its function in yeast. Anc.a localized to both the Golgi/endosomal network and vacuolar membrane and acidified these compartments as part of a hybrid V-ATPase complex. Trafficking of Anc.a did not require retrograde transport from the late endosome to the Golgi that has evolved for retrieval of the Stv1p isoform. Rather, Anc.a localized to both structures through slowed anterograde transport en route to the vacuole. Our results suggest an evolutionary model that describes the differential localization of the two yeast V-ATPase isoforms.

Indexed as

Amino Acid SequenceConsensus SequenceEndosomesGene DeletionGene Knockout TechniquesGolgi ApparatusIntracellular MembranesMolecular Sequence DataProtein IsoformsProtein Structure, TertiaryProtein SubunitsProtein TransportRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentProtein IsoformsProtein SubunitsRecombinant ProteinsSaccharomyces cerevisiae ProteinsVacuolar Proton-Translocating ATPasesV-ATPase a subunit, S cerevisiae

Identifiers

PMID21737673
PMCPMC3164464
OpenAlexW2130439682

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.