Evidence map›Paper›PMID 24196957›Full record

ArticleThe Journal of biological chemistry2013

PAH1-encoded phosphatidate phosphatase plays a role in the growth phase- and inositol-mediated regulation of lipid synthesis in Saccharomyces cerevisiae.

Florencia Pascual, Aníbal Soto-Cardalda, George M Carman

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 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

39 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Architecture and function of yeast phosphatidate phosphatase Pah1 domains/regions.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2024
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Vitamin B3 Biotech · 2023
    Article
  11. Article
  12. Review
  13. A review of phosphatidate phosphatase assays.Journal of lipid research · 2020
    Review
  14. Article
  15. Article
  16. Phosphatidate-mediated regulation of lipid synthesis at the nuclear/endoplasmic reticulum membrane.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020
    Review
  17. Article
  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

3 authors at 1 institution in 1 country.

Florencia PascualFrom the Department of Food Science, Rutgers Center for Lipid Research, and New Jersey Institute for Food, Nutrition, and Health, Rutgers University, New Brunswick, New Jersey 08901.
Aníbal Soto-Cardalda
George M Carman
Rutgers, The State University of New Jersey · US

Funding

Phospholipid metabolism and membrane functionR37GM028140 · NIGMS · RUTGERS, THE STATE UNIV OF N.J. · PI CARMAN, GEORGE M. · 2010 to 2019
$4.0M
PHOSPHOLIPID METABOLSIM AND MEMBRANE FUNCTIONR01GM028140 · NIGMS · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI CARMAN, GEORGE M. · 1985 to 2009
$3.2M
NIGMS NIH HHS GM028140NIGMS NIH HHS R01 GM028140NIGMS NIH HHS R37 GM028140
6 · The paper itself

Abstract

In the yeast Saccharomyces cerevisiae, the synthesis of phospholipids in the exponential phase of growth occurs at the expense of the storage lipid triacylglycerol. As exponential phase cells progress into the stationary phase, the synthesis of triacylglycerol occurs at the expense of phospholipids. Early work indicates a role of the phosphatidate phosphatase (PAP) in this metabolism; the enzyme produces the diacylglycerol needed for the synthesis of triacylglycerol and simultaneously controls the level of phosphatidate for the synthesis of phospholipids. Four genes (APP1, DPP1, LPP1, and PAH1) encode PAP activity in yeast, and it has been unclear which gene is responsible for the synthesis of triacylglycerol throughout growth. An analysis of lipid synthesis and composition, as well as PAP activity in various PAP mutant strains, showed the essential role of PAH1 in triacylglycerol synthesis throughout growth. Pah1p is a phosphorylated enzyme whose in vivo function is dependent on its dephosphorylation by the Nem1p-Spo7p protein phosphatase complex. nem1Δ mutant cells exhibited defects in triacylglycerol synthesis and lipid metabolism that mirrored those imparted by the pah1Δ mutation, substantiating the importance of Pah1p dephosphorylation throughout growth. An analysis of cells bearing PPAH1-lacZ and PPAH1-DPP1 reporter genes showed that PAH1 expression was induced throughout growth and that the induction in the stationary phase was stimulated by inositol supplementation. A mutant analysis indicated that the Ino2p/Ino4p/Opi1p regulatory circuit and transcription factors Gis1p and Rph1p mediated this regulation.

Indexed as

Gene Expression Regulation, FungalGenes, ReporterInositolMembrane ProteinsMutationNuclear ProteinsPhosphatidate PhosphatasePromoter Regions, GeneticSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsTriglyceridesInositolMembrane ProteinsNem1 protein, S cerevisiaeNuclear ProteinsPAH1 protein, S cerevisiaePhosphatidate PhosphataseSaccharomyces cerevisiae ProteinsSPO7 protein, S cerevisiaeTranscription FactorsTriglyceridesDiacylglycerolLipidsPhosphatasePhosphatidatePhospholipidPhospholipid MetabolismTriacylglycerolYeast

Identifiers

PMID24196957
PMCPMC3861629
OpenAlexW2124704338

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.