Evidence map›Paper›PMID 24843009›Full record

ArticleeLife2014

A sphingolipid-dependent diffusion barrier confines ER stress to the yeast mother cell.

Lori Clay, Fabrice Caudron, Annina Denoth-Lippuner, Barbara Boettcher, Stéphanie Buvelot Frei, Erik Lee Snapp, Yves Barral

Open access · goldAbstract read
In one paragraph

Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed
7.1field-weighted citation impact, top 2% 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

93 citing papers in PubMed, 177 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

33 more citing papers are in PubMed but not listed here.

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

7 authors at 2 institutions in 2 countries.

Lori ClayInstitute of Biochemistry, Department of Biology, ETH Zürich, Zürich, Switzerland.
Fabrice CaudronInstitute of Biochemistry, Department of Biology, ETH Zürich, Zürich, Switzerland.
Annina Denoth-LippunerInstitute of Biochemistry, Department of Biology, ETH Zürich, Zürich, Switzerland.
Barbara BoettcherInstitute of Biochemistry, Department of Biology, ETH Zürich, Zürich, Switzerland.
Stéphanie Buvelot FreiInstitute of Biochemistry, Department of Biology, ETH Zürich, Zürich, Switzerland.
Erik Lee SnappDepartment of Anatomy and Structural Biology, Albert Einstein College of Medicine of Yeshiva University, New York, United States.
Yves BarralInstitute of Biochemistry, Department of Biology, ETH Zürich, Zürich, Switzerland yves.barral@bc.biol.ethz.ch.
ETH Zurich · CHAlbert Einstein College of Medicine · US

Funding

Einstein's Nathan Shock Center of Excellence in Basic Biology of AgingP30AG038072 · NIA · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI VIJG, JAN · 2010 to 2024
$10.8M
6 · The paper itself

Abstract

In many cell types, lateral diffusion barriers compartmentalize the plasma membrane and, at least in budding yeast, the endoplasmic reticulum (ER). However, the molecular nature of these barriers, their mode of action and their cellular functions are unclear. Here, we show that misfolded proteins of the ER remain confined into the mother compartment of budding yeast cells. Confinement required the formation of a lateral diffusion barrier in the form of a distinct domain of the ER-membrane at the bud neck, in a septin-, Bud1 GTPase- and sphingolipid-dependent manner. The sphingolipids, but not Bud1, also contributed to barrier formation in the outer membrane of the dividing nucleus. Barrier-dependent confinement of ER stress into the mother cell promoted aging. Together, our data clarify the physical nature of lateral diffusion barriers in the ER and establish the role of such barriers in the asymmetric segregation of proteotoxic misfolded proteins during cell division and aging.DOI: http://dx.doi.org/10.7554/eLife.01883.001.

Indexed as

Cell DivisionEndoplasmic Reticulum StressCell Cycle ProteinsDiffusionEndoplasmic ReticulumGuanine Nucleotide Exchange FactorsIntracellular MembranesMicrofilament ProteinsNuclear EnvelopePermeabilityProtein Foldingrab GTP-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSeptinsSphingolipidsBUD5 protein, S cerevisiaeBUD6 protein, S cerevisiaeCDC24 protein, S cerevisiaeCell Cycle ProteinsGuanine Nucleotide Exchange FactorsMicrofilament Proteinsrab GTP-Binding ProteinsRSR1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSeptinsSphingolipidsagingasymmetric cell divisiondiffusion barrierER stresssphingolipids

Identifiers

PMID24843009
PMCPMC4009826
OpenAlexW2146721676

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.