Evidence map›Paper›PMID 26327557›Full record

ArticlePloS one2015

A Yeast Mutant Deleted of GPH1 Bears Defects in Lipid Metabolism.

Martina Gsell, Ariane Fankl, Lisa Klug, Gerald Mascher, Claudia Schmidt, Claudia Hrastnik, Günther Zellnig, Günther Daum

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

3 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. A TAL effector-like protein of an endofungal bacterium increases the stress tolerance and alters the transcriptome of the host.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  3. 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

8 authors at 2 institutions in 1 country.

Martina GsellInstitute of Biochemistry, Graz University of Technology, NaWi Graz, Petersgasse 12/2, 8010, Graz, Austria.
Ariane FanklInstitute of Biochemistry, Graz University of Technology, NaWi Graz, Petersgasse 12/2, 8010, Graz, Austria.
Lisa KlugInstitute of Biochemistry, Graz University of Technology, NaWi Graz, Petersgasse 12/2, 8010, Graz, Austria.
Gerald MascherInstitute of Biochemistry, Graz University of Technology, NaWi Graz, Petersgasse 12/2, 8010, Graz, Austria.
Claudia SchmidtInstitute of Biochemistry, Graz University of Technology, NaWi Graz, Petersgasse 12/2, 8010, Graz, Austria.
Claudia HrastnikInstitute of Biochemistry, Graz University of Technology, NaWi Graz, Petersgasse 12/2, 8010, Graz, Austria.
Günther ZellnigInstitute of Plant Sciences, Karl Franzens University Graz, NaWi Graz, Austria.
Günther DaumInstitute of Biochemistry, Graz University of Technology, NaWi Graz, Petersgasse 12/2, 8010, Graz, Austria.
Graz University of Technology · ATUniversity of Graz · AT

Funding

Austrian Science Fund FWF P 26133
6 · The paper itself

Abstract

In a previous study we demonstrated up-regulation of the yeast GPH1 gene under conditions of phosphatidylethanolamine (PE) depletion caused by deletion of the mitochondrial (M) phosphatidylserine decarboxylase 1 (PSD1) (Gsell et al., 2013, PLoS One. 8(10):e77380. doi: 10.1371/journal.pone.0077380). Gph1p has originally been identified as a glycogen phosphorylase catalyzing degradation of glycogen to glucose in the stationary growth phase of the yeast. Here we show that deletion of this gene also causes decreased levels of phosphatidylcholine (PC), triacylglycerols and steryl esters. Depletion of the two non-polar lipids in a Δgph1 strain leads to lack of lipid droplets, and decrease of the PC level results in instability of the plasma membrane. In vivo labeling experiments revealed that formation of PC via both pathways of biosynthesis, the cytidine diphosphate (CDP)-choline and the methylation route, is negatively affected by a Δgph1 mutation, although expression of genes involved is not down regulated. Altogether, Gph1p besides its function as a glycogen mobilizing enzyme appears to play a regulatory role in yeast lipid metabolism.

Indexed as

Cell MembraneCytidine Diphosphate CholineEstersGene Expression Regulation, FungalGenes, FungalGlycogenLipid MetabolismMutationPhosphatidylcholinesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTriglyceridesYeastsCytidine Diphosphate CholineEstersGlycogenPhosphatidylcholinesSaccharomyces cerevisiae ProteinsTriglycerides

Identifiers

PMID26327557
PMCPMC4556709
OpenAlexW1931303660

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.