Evidence map›Paper›PMID 20332534›Full record

ArticleThe Journal of biological chemistry2010

Multiple functions as lipase, steryl ester hydrolase, phospholipase, and acyltransferase of Tgl4p from the yeast Saccharomyces cerevisiae.

Sona Rajakumari, Günther Daum

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
5.5field-weighted citation impact, top 4% 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

31 citing papers in PubMed, 92 citations in OpenAlex.

  1. Article
  2. Engineering yeast for tailored fatty acid profiles.Applied microbiology and biotechnology · 2025
    Review
  3. Article
  4. Article
  5. Phosphatidic acid biosynthesis in the model organism yeast Saccharomyces cerevisiae - a survey.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2021
    Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Computational Modeling of Lipid Metabolism in Yeast.Frontiers in molecular biosciences · 2016
    Article
  14. Morphogenesis checkpoint kinase Swe1 is the executor of lipolysis-dependent cell-cycle progression.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

Sona RajakumariInstitute of Biochemistry, Graz University of Technology, A-8010 Graz, Austria.
Günther Daum
Graz University of Technology · AT

Funding

Austrian Science Fund FWF W 901
6 · The paper itself

Abstract

Triacylglycerol (TAG) hydrolysis, membrane lipid biosynthesis, and lipid turnover are largely interlinked processes. In yeast, TAG is mobilized by three TAG lipases named Tgl3p, Tgl4p, and Tgl5p, which are localized to lipid particles/droplets. These TAG lipases posses a conserved GXSXG motif that is characteristic of hydrolytic enzymes. Here, we demonstrated that the yeast TAG lipase Tgl4p, the functional ortholog of the adipose TAG lipase, ATGL, catalyzes multiple functions in lipid metabolism. An extended domain and motif search analysis revealed that Tgl4p bears not only a lipase consensus domain but also a conserved motif for calcium-independent phospholipase A(2). We show that Tgl4p exhibits TAG lipase, steryl ester hydrolase, and phospholipase A(2) activities, but surprisingly it also catalyzed the acyl-CoA-dependent acylation of lysophosphatidic acid to phosphatidic acid (PA). Heterologous overexpression of Tgl4p in Pichia pastoris increased total phospholipid and specifically PA synthesis. Moreover, deletion of TGL4 in Saccharomyces cerevisiae showed an altered pattern of phosphatidylcholine and PA molecular species. Altogether, our data suggest that yeast Tgl4p functions as a hydrolytic enzyme in lipid degradation but also contributes to fatty acid channeling and phospholipid remodeling.

Indexed as

AcylationAcyltransferasesAmino Acid MotifsGene DeletionLipaseLipid MetabolismLysophospholipidsPhosphatidic AcidsPhosphatidylcholinesPhospholipases A2Protein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSterol EsteraseTriglyceridesAcyltransferasesLipaselysophosphatidic acidLysophospholipidsPhosphatidic AcidsPhosphatidylcholinesPhospholipases A2Saccharomyces cerevisiae ProteinsSterol EsteraseTgl4 protein, S cerevisiaeTriglycerides

Identifiers

PMID20332534
PMCPMC2871444
OpenAlexW2032087664

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.