Evidence map›Paper›PMID 27758859›Full record

ArticleThe Journal of biological chemistry2016

Cloning of Glycerophosphocholine Acyltransferase (GPCAT) from Fungi and Plants: A NOVEL ENZYME IN PHOSPHATIDYLCHOLINE SYNTHESIS.

Bartosz Głąb, Mirela Beganovic, Sanket Anaokar, Meng-Shu Hao, Allan G Rasmusson, Jana Patton-Vogt, Antoni Banaś, Sten Stymne, Ida Lager

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.2field-weighted citation impact, top 14% 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

17 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Functional Prediction ofMembranes · 2026
    Article
  3. Article
  4. Review
  5. Phosphatidylcholine biosynthesis pathways inFrontiers in cellular and infection microbiology · 2025
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Phospholipid turnover and acyl chain remodeling in the yeast ER.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020
    Review
  14. Article
  15. Article
  16. Article
  17. 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

9 authors at 4 institutions in 3 countries.

Bartosz GłąbFrom the Intercollegiate Faculty of Biotechnology, University of Gdańsk and Medical University of Gdańsk, 80-822 Gdańsk, Poland.
Mirela Beganovicthe Department of Plant Breeding, Swedish University of Agricultural Sciences, 230 53 Alnarp, Sweden.
Sanket Anaokarthe Department of Biological Sciences, Duquesne University, Pittsburgh, Pennsylvania 15282, and.
Meng-Shu Haothe Department of Biology, Lund University, Biology Building A, Sölvegatan 35, 223 62 Lund, Sweden.
Allan G Rasmussonthe Department of Biology, Lund University, Biology Building A, Sölvegatan 35, 223 62 Lund, Sweden.
Jana Patton-Vogtthe Department of Biological Sciences, Duquesne University, Pittsburgh, Pennsylvania 15282, and.
Antoni BanaśFrom the Intercollegiate Faculty of Biotechnology, University of Gdańsk and Medical University of Gdańsk, 80-822 Gdańsk, Poland.
Sten Stymnethe Department of Plant Breeding, Swedish University of Agricultural Sciences, 230 53 Alnarp, Sweden.
Ida Lagerthe Department of Plant Breeding, Swedish University of Agricultural Sciences, 230 53 Alnarp, Sweden, ida.lager@slu.se.ORCID http://orcid.org/0000-0001-9755-8534
Swedish University of Agricultural Sciences · SEDuquesne University · USGdańsk Medical University · PLLund University · SE

Funding

The Role of Phospholipid Turnover in Membrane Protein FunctionR15GM104876 · NIGMS · DUQUESNE UNIVERSITY · PI VOGT, JANA L · 2013 to 2024
$1.3M
NIGMS NIH HHS R15 GM104876
6 · The paper itself

Abstract

Glycero-3-phosphocholine (GPC), the product of the complete deacylation of phosphatidylcholine (PC), was long thought to not be a substrate for reacylation. However, it was recently shown that cell-free extracts from yeast and plants could acylate GPC with acyl groups from acyl-CoA. By screening enzyme activities of extracts derived from a yeast knock-out collection, we were able to identify and clone the yeast gene (GPC1) encoding the enzyme, named glycerophosphocholine acyltransferase (GPCAT). By homology search, we also identified and cloned GPCAT genes from three plant species. All enzymes utilize acyl-CoA to acylate GPC, forming lyso-PC, and they show broad acyl specificities in both yeast and plants. In addition to acyl-CoA, GPCAT efficiently utilizes LPC and lysophosphatidylethanolamine as acyl donors in the acylation of GPC. GPCAT homologues were found in the major eukaryotic organism groups but not in prokaryotes or chordates. The enzyme forms its own protein family and does not contain any of the acyl binding or lipase motifs that are present in other studied acyltransferases and transacylases. In vivo labeling studies confirm a role for Gpc1p in PC biosynthesis in yeast. It is postulated that GPCATs contribute to the maintenance of PC homeostasis and also have specific functions in acyl editing of PC (e.g. in transferring acyl groups modified at the sn-2 position of PC to the sn-1 position of this molecule in plant cells).

Indexed as

AcylationAcyl Coenzyme AAcyltransferasesPhosphatidylcholinesPlant ProteinsPlantsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAcyl Coenzyme AAcyltransferasesglycerophosphocholine acyltransferase, S cerevisiaePhosphatidylcholinesPlant ProteinsSaccharomyces cerevisiae Proteinsacyltransferaseglycerophospholipidlipid metabolismphosphatidylcholineplant biochemistry

Identifiers

PMID27758859
PMCPMC5122774
OpenAlexW2528738067

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.