Evidence map›Paper›PMID 22496448›Full record

ArticleThe Journal of biological chemistry2012

Sorting of the yeast vacuolar-type, proton-translocating ATPase enzyme complex (V-ATPase): identification of a necessary and sufficient Golgi/endosomal retention signal in Stv1p.

Gregory C Finnigan, Glen E Cronan, Hae J Park, Sankaranarayanan Srinivasan, Florante A Quiocho, Tom H Stevens

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

36 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
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  4. Article
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  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. The Plant V-ATPase.Frontiers in plant science · 2022
    Review
  12. Article
  13. The V-ATPaseInternational journal of molecular sciences · 2021
    Review
  14. A capsule-associated gene ofMicrobiology (Reading, England) · 2021
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. 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

6 authors at 2 institutions in 1 country.

Gregory C FinniganInstitute of Molecular Biology, University of Oregon, Eugene, Oregon 97403, USA.
Glen E Cronan
Hae J Park
Sankaranarayanan Srinivasan
Florante A Quiocho
Tom H Stevens
University of Oregon · USBaylor College of Medicine · US

Funding

Graduate Training in Genetics Administrative Supplement - Career Curriculum DevelopmentT32GM007413 · NIGMS · UNIVERSITY OF OREGON · PI GUILLEMIN, KAREN J · 1985 to 2022
$7.8M
SORTING AND TRANSPORT OF YEAST MEMBRANE PROTEINSR01GM038006 · NIGMS · UNIVERSITY OF OREGON · PI STEVENS, TOM HALL · 1987 to 2016
$4.9M
Molecular Studies of the Roles and Regulations of the v-ATPase V0 SectorR01GM088803 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI QUIOCHO, FLORANTE A · 2009 to 2010
$971k
NIGMS NIH HHS GM088803NIGMS NIH HHS GM38006NIGMS NIH HHS R01 GM038006NIGMS NIH HHS R01 GM088803NIGMS NIH HHS T32 GM007413
6 · The paper itself

Abstract

Subunit a of the yeast vacuolar-type, proton-translocating ATPase enzyme complex (V-ATPase) is responsible for both proton translocation and subcellular localization of this highly conserved molecular machine. Inclusion of the Vph1p isoform causes the V-ATPase complex to traffic to the vacuolar membrane, whereas incorporation of Stv1p causes continued cycling between the trans-Golgi and endosome. We previously demonstrated that this targeting information is contained within the cytosolic, N-terminal portion of V-ATPase subunit a (Stv1p). To identify residues responsible for sorting of the Golgi isoform of the V-ATPase, a random mutagenesis was performed on the N terminus of Stv1p. Subsequent characterization of mutant alleles led to the identification of a short peptide sequence, W(83)KY, that is necessary for proper Stv1p localization. Based on three-dimensional homology modeling to the Meiothermus ruber subunit I, we propose a structural model of the intact Stv1p-containing V-ATPase demonstrating the accessibility of the W(83)KY sequence to retrograde sorting machinery. Finally, we characterized the sorting signal within the context of a reconstructed Stv1p ancestor (Anc.Stv1). This evolutionary intermediate includes an endogenous W(83)KY sorting motif and is sufficient to compete with sorting of the native yeast Stv1p V-ATPase isoform. These data define a novel sorting signal that is both necessary and sufficient for trafficking of the V-ATPase within the Golgi/endosomal network.

Indexed as

Amino Acid MotifsEndosomesEvolution, MolecularIsoenzymesModels, MolecularProtein Sorting SignalsProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStructural Homology, Proteintrans-Golgi NetworkVacuolar Proton-Translocating ATPasesIsoenzymesProtein Sorting SignalsSaccharomyces cerevisiae ProteinsVacuolar Proton-Translocating ATPases

Identifiers

PMID22496448
PMCPMC3365986
OpenAlexW2066945058

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.