Evidence map›Paper›PMID 24187129›Full record

ArticleThe Journal of biological chemistry2013

Screening for hydrolytic enzymes reveals Ayr1p as a novel triacylglycerol lipase in Saccharomyces cerevisiae.

Birgit Ploier, Melanie Scharwey, Barbara Koch, Claudia Schmidt, Jessica Schatte, Gerald Rechberger, Manfred Kollroser, Albin Hermetter, Günther Daum

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

20 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Phosphatidic acid biosynthesis in the model organism yeast Saccharomyces cerevisiae - a survey.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2021
    Review
  8. Article
  9. Metabolic engineering ofMetabolic engineering communications · 2018
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Lipid droplet dynamics in budding yeast.Cellular and molecular life sciences : CMLS · 2015
    Review
  19. Article
  20. 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

9 authors at 3 institutions in 1 country.

Birgit PloierFrom the Institute of Biochemistry, Graz University of Technology, Petersgasse 12/2, A-8010 Graz, Austria.
Melanie Scharwey
Barbara Koch
Claudia Schmidt
Jessica Schatte
Gerald Rechberger
Manfred Kollroser
Albin Hermetter
Günther Daum
Graz University of Technology · ATMedical University of Graz · ATUniversity of Graz · AT

Funding

Austrian Science Fund FWF P 23029
6 · The paper itself

Abstract

Saccharomyces cerevisiae, as well as other eukaryotes, preserves fatty acids and sterols in a biologically inert form, as triacylglycerols and steryl esters. The major triacylglycerol lipases of the yeast S. cerevisiae identified so far are Tgl3p, Tgl4p, and Tgl5p (Athenstaedt, K., and Daum, G. (2003) YMR313c/TGL3 encodes a novel triacylglycerol lipase located in lipid particles of Saccharomyces cerevisiae. J. Biol. Chem. 278, 23317-23323; Athenstaedt, K., and Daum, G. (2005) Tgl4p and Tgl5p, two triacylglycerol lipases of the yeast Saccharomyces cerevisiae, are localized to lipid particles. J. Biol. Chem. 280, 37301-37309). We observed that upon cultivation on oleic acid, triacylglycerol mobilization did not come to a halt in a yeast strain deficient in all currently known triacylglycerol lipases, indicating the presence of additional not yet characterized lipases/esterases. Functional proteome analysis using lipase and esterase inhibitors revealed a subset of candidate genes for yet unknown hydrolytic enzymes on peroxisomes and lipid droplets. Based on the conserved GXSXG lipase motif, putative functions, and subcellular localizations, a selected number of candidates were characterized by enzyme assays in vitro, gene expression analysis, non-polar lipid analysis, and in vivo triacylglycerol mobilization assays. These investigations led to the identification of Ayr1p as a novel triacylglycerol lipase of yeast lipid droplets and confirmed the hydrolytic potential of the peroxisomal Lpx1p in vivo. Based on these results, we discuss a possible link between lipid storage, lipid mobilization, and peroxisomal utilization of fatty acids as a carbon source.

Indexed as

Biological TransportCarboxylic Ester HydrolasesCulture MediaGene Expression Regulation, FungalHydrolysisLipaseOleic AcidSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSugar Alcohol DehydrogenasesTriglyceridesacylglycerone-phosphate reductaseAyr1 protein, S cerevisiaeCarboxylic Ester HydrolasesCulture MediaLipaseOleic AcidSaccharomyces cerevisiae ProteinsSugar Alcohol DehydrogenasesTriglyceridesLipaseLipid DropletsLipidsPeroxisomesTriacylglycerolYeast

Identifiers

PMID24187129
PMCPMC3861654
OpenAlexW2079481813

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.