Evidence map›Paper›PMID 25713391›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Morphogenesis checkpoint kinase Swe1 is the executor of lipolysis-dependent cell-cycle progression.

Neha Chauhan, Myriam Visram, Alvaro Cristobal-Sarramian, Florian Sarkleti, Sepp D Kohlwein

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

15 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Yeast Sphingolipid Phospholipase GeneMolecular and cellular biology · 2020
    Article
  8. Review
  9. Article
  10. Sphingolipids and their metabolism in physiology and disease.Nature reviews. Molecular cell biology · 2018
    Review
  11. Establishing the lipid droplet proteome: Mechanisms of lipid droplet protein targeting and degradation.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017
    Review
  12. Article
  13. Review
  14. Article
  15. New role for ceramide in the pheromone response.Cell cycle (Georgetown, Tex.) · 2016
    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

5 authors at 1 institution in 1 country.

Neha ChauhanInstitute of Molecular Biosciences, BioTechMed Graz, University of Graz, A8010 Graz, Austria.
Myriam VisramInstitute of Molecular Biosciences, BioTechMed Graz, University of Graz, A8010 Graz, Austria.
Alvaro Cristobal-SarramianInstitute of Molecular Biosciences, BioTechMed Graz, University of Graz, A8010 Graz, Austria.
Florian SarkletiInstitute of Molecular Biosciences, BioTechMed Graz, University of Graz, A8010 Graz, Austria.
Sepp D KohlweinInstitute of Molecular Biosciences, BioTechMed Graz, University of Graz, A8010 Graz, Austria sepp.kohlwein@uni-graz.at.ORCID http://orcid.org/0000-0002-1030-0598
University of Graz · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cell growth and division requires the precise duplication of cellular DNA content but also of membranes and organelles. Knowledge about the cell-cycle-dependent regulation of membrane and storage lipid homeostasis is only rudimentary. Previous work from our laboratory has shown that the breakdown of triacylglycerols (TGs) is regulated in a cell-cycle-dependent manner, by activation of the Tgl4 lipase by the major cyclin-dependent kinase Cdc28. The lipases Tgl3 and Tgl4 are required for efficient cell-cycle progression during the G1/S (Gap1/replication phase) transition, at the onset of bud formation, and their absence leads to a cell-cycle delay. We now show that defective lipolysis activates the Swe1 morphogenesis checkpoint kinase that halts cell-cycle progression by phosphorylation of Cdc28 at tyrosine residue 19. Saturated long-chain fatty acids and phytosphingosine supplementation rescue the cell-cycle delay in the Tgl3/Tgl4 lipase-deficient strain, suggesting that Swe1 activity responds to imbalanced sphingolipid metabolism, in the absence of TG degradation. We propose a model by which TG-derived sphingolipids are required to activate the protein phosphatase 2A (PP2A(Cdc55)) to attenuate Swe1 phosphorylation and its inhibitory effect on Cdc28 at the G1/S transition of the cell cycle.

Indexed as

MorphogenesisBase SequenceBiocatalysisCell CycleCell Cycle ProteinsDNA PrimersLipaseLipolysisProtein-Tyrosine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCell Cycle ProteinsDNA PrimersLipaseProtein-Tyrosine KinasesSaccharomyces cerevisiae ProteinsSWE1 protein, S cerevisiaeTGL3 protein, S cerevisiaeTgl4 protein, S cerevisiaecyclin-dependent kinaseG1/S transitionlipasesphingolipidtriglyceride

Identifiers

PMID25713391
PMCPMC4364240
OpenAlexW1979124782

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.