Evidence map›Paper›PMID 22910056›Full record

ReviewBiochimica et biophysica acta2013

Phosphatidate phosphatase, a key regulator of lipid homeostasis.

Florencia Pascual, George M Carman

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed
7.7field-weighted citation impact, top 2% 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

86 citing papers in PubMed, 158 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Architecture and function of yeast phosphatidate phosphatase Pah1 domains/regions.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2024
    Review
  8. Review
  9. Article
  10. Article
  11. A Yeast Mitotic Tale for the Nucleus and the Vacuoles to Embrace.International journal of molecular sciences · 2023
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

26 more citing papers are in PubMed but not listed here.

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 2 institutions in 2 countries.

Florencia PascualDepartment of Food Science and Rutgers Center for Lipid Research, Rutgers University, New Brunswick, NJ 08901, USA. fpascual@eden.rutgers.edu
George M Carman
Rutgers Sexual and Reproductive Health and Rights · NLRutgers, The State University of New Jersey · US

Funding

REGULATION OF PHOSPHOLIPID SYNTHESIS BY CTPR01GM050679 · NIGMS · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI CARMAN, GEORGE M. · 1994 to 2019
$6.0M
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
STRUCTURE OF HEMOCYANINR01GM028410 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI RIGGS, AUSTEN F · 1985 to 1985
–
NIGMS NIH HHS GM-28410NIGMS NIH HHS GM-50679NIGMS NIH HHS R01 GM028140NIGMS NIH HHS R01 GM050679NIGMS NIH HHS R37 GM028140
6 · The paper itself

Abstract

Yeast Pah1p phosphatidate phosphatase (PAP) catalyzes the penultimate step in the synthesis of triacylglycerol. PAP plays a crucial role in lipid homeostasis by controlling the relative proportions of its substrate phosphatidate and its product diacylglycerol. The cellular amounts of these lipid intermediates influence the synthesis of triacylglycerol and the pathways by which membrane phospholipids are synthesized. Physiological functions affected by PAP activity include phospholipid synthesis gene expression, nuclear/endoplasmic reticulum membrane growth, lipid droplet formation, and vacuole homeostasis and fusion. Yeast lacking Pah1p PAP activity are acutely sensitive to fatty acid-induced toxicity and exhibit respiratory deficiency. PAP is distinguished in its cellular location, catalytic mechanism, and physiological functions from Dpp1p and Lpp1p lipid phosphate phosphatases that utilize a variety of substrates that include phosphatidate. Phosphorylation/dephosphorylation is a major mechanism by which Pah1p PAP activity is regulated. Pah1p is phosphorylated by cytosolic-associated Pho85p-Pho80p, Cdc28p-cyclin B, and protein kinase A and is dephosphorylated by the endoplasmic reticulum-associated Nem1p-Spo7p phosphatase. The dephosphorylation of Pah1p stimulates PAP activity and facilitates the association with the membrane/phosphatidate allowing for its reaction and triacylglycerol synthesis. This article is part of a Special Issue entitled Phospholipids and Phospholipid Metabolism.

Indexed as

AnimalsCyclic AMP-Dependent Protein KinasesCyclin-Dependent KinasesDiglyceridesGene Expression Regulation, FungalLipid MetabolismMembrane ProteinsNuclear ProteinsPhosphatidate PhosphatasePhosphatidic AcidsPhosphorylationPyrophosphatasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTriglycerides1,2-diacylglycerolCyclic AMP-Dependent Protein KinasesCyclin-Dependent KinasesDiglyceridesDPP1 protein, S cerevisiaelipid phosphate phosphataseMembrane ProteinsNem1 protein, S cerevisiaeNuclear ProteinsPAH1 protein, S cerevisiaePhosphatidate PhosphatasePhosphatidic AcidsPyrophosphatasesSaccharomyces cerevisiae ProteinsTriglycerides

Identifiers

PMID22910056
PMCPMC3549317
OpenAlexW2062279991

What OpenQuestion holds

Textmetadata
LicenceTDM
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.