Evidence map›Paper›PMID 35766971›Full record

ArticleThe Journal of cell biology2022

Cvm1 is a component of multiple vacuolar contact sites required for sphingolipid homeostasis.

Daniel D Bisinski, Inês Gomes Castro, Muriel Mari, Stefan Walter, Florian Fröhlich, Maya Schuldiner, Ayelén González Montoro

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

13 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Review
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  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. The Vacuole Lipid Droplet Contact Site vCLIP.Contact (Thousand Oaks (Ventura County, Calif.))
    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

7 authors at 3 institutions in 3 countries.

Daniel D BisinskiDepartment of Biology/Chemistry, Cellular Communication Laboratory, University of Osnabrück, Osnabrück, Germany.ORCID 0000-0001-6762-5070
Inês Gomes CastroDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot, Israel.ORCID 0000-0003-4669-985X
Muriel MariDepartment of Biomedical Sciences of Cells and Systems, University of Groningen, University Medical Center Groningen, Groningen, Netherlands.ORCID 0000-0002-2677-6945
Stefan WalterCenter of Cellular Nanoanalytics Osnabrück, Osnabrück, Germany.
Florian FröhlichCenter of Cellular Nanoanalytics Osnabrück, Osnabrück, Germany.ORCID 0000-0001-8307-2189
Maya SchuldinerDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot, Israel.ORCID 0000-0001-9947-115X
Ayelén González MontoroDepartment of Biology/Chemistry, Cellular Communication Laboratory, University of Osnabrück, Osnabrück, Germany.ORCID 0000-0002-6978-8284
Osnabrück University · DEWeizmann Institute of Science · ILUniversity Medical Center Groningen · NL

Funding

Deutsche Forschungsgemeinschaft SFB944Dutch Research Council ALWOP.355European Molecular Biology Organization aALTF 609-2018Schering and Fritz Thyssen Foundations 20.18.0.029MNVolkswagen Foundation 93092MS
6 · The paper itself

Abstract

Membrane contact sites are specialized platforms formed between most organelles that enable them to exchange metabolites and influence the dynamics of each other. The yeast vacuole is a degradative organelle equivalent to the lysosome in higher eukaryotes with important roles in ion homeostasis and metabolism. Using a high-content microscopy screen, we identified Ymr160w (Cvm1, for contact of the vacuole membrane 1) as a novel component of three different contact sites of the vacuole: with the nuclear endoplasmic reticulum, the mitochondria, and the peroxisomes. At the vacuole-mitochondria contact site, Cvm1 acts as a tether independently of previously known tethers. We show that changes in Cvm1 levels affect sphingolipid homeostasis, altering the levels of multiple sphingolipid classes and the response of sphingolipid-sensing signaling pathways. Furthermore, the contact sites formed by Cvm1 are induced upon a decrease in sphingolipid levels. Altogether, our work identifies a novel protein that forms multiple contact sites and supports a role of lysosomal contacts in sphingolipid homeostasis.

Indexed as

Saccharomyces cerevisiae ProteinsSphingolipidsVacuolesHomeostasisSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSphingolipids

Identifiers

PMID35766971
PMCPMC9247719
OpenAlexW4283735268

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.