Evidence map›Paper›PMID 21071438›Full record

ArticleThe Journal of biological chemistry2011

DGK1-encoded diacylglycerol kinase activity is required for phospholipid synthesis during growth resumption from stationary phase in Saccharomyces cerevisiae.

Stylianos Fakas, Chrysanthos Konstantinou, George M Carman

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

41 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Elevating Phospholipids ProductionInternational journal of molecular sciences · 2022
    Article
  6. Article
  7. Article
  8. Phosphatidate-mediated regulation of lipid synthesis at the nuclear/endoplasmic reticulum membrane.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020
    Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Lipid metabolic changes in an early divergent fungus govern the establishment of a mutualistic symbiosis with endobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  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

3 authors at 1 institution in 1 country.

Stylianos FakasDepartment of Food Science and Rutgers Center for Lipid Research, Rutgers University, New Brunswick, New Jersey 08901, USA.
Chrysanthos Konstantinou
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 GM-28140NIGMS NIH HHS R01 GM028140NIGMS NIH HHS R37 GM028140
6 · The paper itself

Abstract

In the yeast Saccharomyces cerevisiae, triacylglycerol mobilization for phospholipid synthesis occurs during growth resumption from stationary phase, and this metabolism is essential in the absence of de novo fatty acid synthesis. In this work, we provide evidence that DGK1-encoded diacylglycerol kinase activity is required to convert triacylglycerol-derived diacylglycerol to phosphatidate for phospholipid synthesis. Cells lacking diacylglycerol kinase activity (e.g. dgk1Δ mutation) failed to resume growth in the presence of the fatty acid synthesis inhibitor cerulenin. Lipid analysis data showed that dgk1Δ mutant cells did not mobilize triacylglycerol for membrane phospholipid synthesis and accumulated diacylglycerol. The dgk1Δ phenotypes were partially complemented by preventing the formation of diacylglycerol by the PAH1-encoded phosphatidate phosphatase and by channeling diacylglycerol to phosphatidylcholine via the Kennedy pathway. These observations, coupled to an inhibitory effect of dioctanoyl-diacylglycerol on the growth of wild type cells, indicated that diacylglycerol kinase also functions to alleviate diacylglycerol toxicity.

Indexed as

CeruleninCholineDiacylglycerol KinaseDiglyceridesGene DeletionPhosphatidate PhosphatasePhospholipidsRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCeruleninCholineDGK1 protein, S cerevisiaeDiacylglycerol KinaseDiglyceridesPAH1 protein, S cerevisiaePhosphatidate PhosphatasePhospholipidsRepressor ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID21071438
PMCPMC3020755
OpenAlexW2106308853

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.