Evidence map›Paper›PMID 25862304›Full record

ArticleThe Plant cell2015

PHOSPHATIDIC ACID PHOSPHOHYDROLASE Regulates Phosphatidylcholine Biosynthesis in Arabidopsis by Phosphatidic Acid-Mediated Activation of CTP:PHOSPHOCHOLINE CYTIDYLYLTRANSFERASE Activity.

Christian P Craddock, Nicolette Adams, Fiona M Bryant, Smita Kurup, Peter J Eastmond

Open access · hybridAbstract read
In one paragraph

Article in The Plant cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
4.5field-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

34 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
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  6. Article
  7. Article
  8. Rice lipases: a conundrum in rice bran stabilization: a review on their impact and biotechnological interventions.Physiology and molecular biology of plants : an international journal of functional plant biology · 2023
    Review
  9. RNA-seq profiling in leaf tissues of two soybean (Molecular breeding : new strategies in plant improvement · 2023
    Article
  10. Article
  11. Review
  12. The Delay ofPlants (Basel, Switzerland) · 2022
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. The Journal of biological chemistry · 2019
    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

5 authors at 2 institutions in 1 country.

Christian P CraddockSchool of Life Sciences, University of Warwick, Coventry CV4 7AL, United Kingdom.
Nicolette AdamsSchool of Life Sciences, University of Warwick, Coventry CV4 7AL, United Kingdom.
Fiona M BryantDepartment of Plant Biology and Crop Science, Rothamsted Research, Harpenden, Hertfordshire AL5 2JQ, United Kingdom.
Smita KurupDepartment of Plant Biology and Crop Science, Rothamsted Research, Harpenden, Hertfordshire AL5 2JQ, United Kingdom.
Peter J EastmondDepartment of Plant Biology and Crop Science, Rothamsted Research, Harpenden, Hertfordshire AL5 2JQ, United Kingdom peter.eastmond@rothamsted.ac.uk.
Rothamsted Research · GBUniversity of Warwick · GB

Funding

Biotechnology and Biological Sciences Research Council BB/G009724/1Biotechnology and Biological Sciences Research Council BBS/E/C/00005207
6 · The paper itself

Abstract

Regulation of membrane lipid biosynthesis is critical for cell function. We previously reported that disruption of PHOSPHATIDIC ACID PHOSPHOHYDROLASE1 (PAH1) and PAH2 stimulates net phosphatidylcholine (PC) biosynthesis and proliferation of the endoplasmic reticulum (ER) in Arabidopsis thaliana. Here, we show that this response is caused specifically by a reduction in the catalytic activity of the protein and positively correlates with an accumulation of its substrate, phosphatidic acid (PA). The accumulation of PC in pah1 pah2 is suppressed by disruption of CTP:PHOSPHOCHOLINE CYTIDYLYLTRANSFERASE1 (CCT1), which encodes a key enzyme in the nucleotide pathway for PC biosynthesis. The activity of recombinant CCT1 is stimulated by lipid vesicles containing PA. Truncation of CCT1, to remove the predicted C-terminal amphipathic lipid binding domain, produced a constitutively active enzyme. Overexpression of native CCT1 in Arabidopsis has no significant effect on PC biosynthesis or ER morphology, but overexpression of the truncated constitutively active version largely replicates the pah1 pah2 phenotype. Our data establish that membrane homeostasis is regulated by lipid composition in Arabidopsis and reveal a mechanism through which the abundance of PA, mediated by PAH activity, modulates CCT activity to govern PC content.

Indexed as

ArabidopsisArabidopsis ProteinsCholine-Phosphate CytidylyltransferasePhosphatidate PhosphatasePhosphorylcholineArabidopsis ProteinsCCT1 protein, ArabidopsisCholine-Phosphate CytidylyltransferasePhosphatidate PhosphatasePhosphorylcholine

Identifiers

PMID25862304
PMCPMC4558698
OpenAlexW2011632041

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.