Evidence map›Paper›PMID 26466677›Full record

ArticleMolecular biology of the cell2015

Target of rapamycin signaling mediates vacuolar fission caused by endoplasmic reticulum stress in Saccharomyces cerevisiae.

Bobbiejane Stauffer, Ted Powers

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2015. 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
1.7field-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

18 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Treatment ofFrontiers in toxicology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. 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

2 authors at 1 institution in 1 country.

Bobbiejane StaufferDepartment of Molecular and Cellular Biology, College of Biological Sciences, University of California, Davis, Davis, CA 95616.
Ted PowersDepartment of Molecular and Cellular Biology, College of Biological Sciences, University of California, Davis, Davis, CA 95616 tpowers@ucdavis.edu).
University of California, Davis · US

Funding

TOR Complex 2 and sphingolipid biosynthesis.R01GM086387 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI POWERS, TED · 2009 to 2012
$1.3M
NIGMS NIH HHS GM086387NIGMS NIH HHS R01 GM086387
6 · The paper itself

Abstract

The yeast vacuole is equivalent to the mammalian lysosome and, in response to diverse physiological and environmental stimuli, undergoes alterations both in size and number. Here we demonstrate that vacuoles fragment in response to stress within the endoplasmic reticulum (ER) caused by chemical or genetic perturbations. We establish that this response does not involve known signaling pathways linked previously to ER stress but instead requires the rapamycin-sensitive TOR Complex 1 (TORC1), a master regulator of cell growth, together with its downstream effectors, Tap42/Sit4 and Sch9. To identify additional factors required for ER stress-induced vacuolar fragmentation, we conducted a high-throughput, genome-wide visual screen for yeast mutants that are refractory to ER stress-induced changes in vacuolar morphology. We identified several genes shown previously to be required for vacuolar fusion and/or fission, validating the utility of this approach. We also identified a number of new components important for fragmentation, including a set of proteins involved in assembly of the V-ATPase. Remarkably, we find that one of these, Vph2, undergoes a change in intracellular localization in response to ER stress and, moreover, in a manner that requires TORC1 activity. Together these results reveal a new role for TORC1 in the regulation of vacuolar behavior.

Indexed as

Adaptor Proteins, Signal TransducingCell ProliferationEndoplasmic ReticulumEndoplasmic Reticulum StressMembrane ProteinsMolecular ChaperonesProtein Serine-Threonine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionTranscription FactorsVacuolesAdaptor Proteins, Signal TransducingMembrane ProteinsMolecular ChaperonesProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsSCH9 protein, S cerevisiaeTAP42 protein, S cerevisiaeTORC1 protein complex, S cerevisiaeTranscription FactorsVPH2 protein, S cerevisiae

Identifiers

PMID26466677
PMCPMC4678019
OpenAlexW2220883082

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.