Evidence map›Paper›PMID 20554061›Full record

ArticleBiochimica et biophysica acta2010

Identification of Yju3p as functional orthologue of mammalian monoglyceride lipase in the yeast Saccharomycescerevisiae.

Christoph Heier, Ulrike Taschler, Srinivasan Rengachari, Monika Oberer, Heimo Wolinski, Klaus Natter, Sepp D Kohlwein, Regina Leber, Robert Zimmermann

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

26 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
  2. Engineering yeast for tailored fatty acid profiles.Applied microbiology and biotechnology · 2025
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  5. Metabolic, Organoleptic and Transcriptomic Impact ofInternational journal of molecular sciences · 2021
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  7. Tapetal Expression ofFrontiers in plant science · 2019
    Article
  8. Review
  9. Article
  10. Lipid droplet dynamics in budding yeast.Cellular and molecular life sciences : CMLS · 2015
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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 1 institution in 1 country.

Christoph HeierInstitute of Molecular Biosciences, University of Graz, Humboldtstrasse 50, A-8010 Graz, Austria.
Ulrike Taschler
Srinivasan Rengachari
Monika Oberer
Heimo Wolinski
Klaus Natter
Sepp D Kohlwein
Regina Leber
Robert Zimmermann
University of Graz · AT

Funding

Austrian Science Fund FWF P 21296Austrian Science Fund FWF W 901
6 · The paper itself

Abstract

Monoacylglycerols (MAGs) are short-lived intermediates of glycerolipid metabolism. Specific molecular species, such as 2-arachidonoylglycerol, which is a potent activator of cannabinoid receptors, may also function as lipid signaling molecules. In mammals, enzymes hydrolyzing MAG to glycerol and fatty acids, resembling the final step in lipolysis, or esterifying MAG to diacylglycerol, are well known; however, despite the high level of conservation of lipolysis, the corresponding activities in yeast have not been characterized yet. Here we provide evidence that the protein Yju3p functions as a potent MAG hydrolase in yeast. Cellular MAG hydrolase activity was decreased by more than 90% in extracts of Yju3p-deficient cells, indicating that Yju3p accounts for the vast majority of this activity in yeast. Loss of this activity was restored by heterologous expression of murine monoglyceride lipase (MGL). Since yju3Delta mutants accumulated MAG in vivo only at very low concentrations, we considered the possibility that MAGs are re-esterified into DAG by acyltransferases. Indeed, cellular MAG levels were further increased in mutant cells lacking Yju3p and Dga1p or Lro1p acyltransferase activities. In conclusion, our studies suggest that catabolic and anabolic reactions affect cellular MAG levels. Yju3p is the functional orthologue of mammalian MGL and is required for efficient degradation of MAG in yeast.

Indexed as

AcyltransferasesAmino Acid SequenceAnimalsCloning, MolecularDiacylglycerol O-AcyltransferaseGenetic Complementation TestHydrolysisMiceMolecular Sequence DataMonoacylglycerol LipasesMonoglyceridesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidSubcellular FractionsTriglyceridesAcyltransferasesDGA1 protein, S cerevisiaeDiacylglycerol O-AcyltransferaseMonoacylglycerol LipasesMonoglyceridesSaccharomyces cerevisiae ProteinsTriglyceridesYju3 protein, S cerevisiae

Identifiers

PMID20554061
PMCPMC2911655
OpenAlexW2070767090

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.