Evidence map›Paper›PMID 40561507›Full record

ArticlePlant physiology2025

Functions of Arabidopsis CTP:phosphocholine cytidylyltransferase 1 in phosphatidylcholine biosynthesis and root growth.

Qiong Xiao, Daniel Bustos, Kristian M Caldo, Luis Morales-Quintana, Tao Huan, Guanqun Chen

Abstract read
In one paragraph

Article in Plant physiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
  2. 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

6 authors.

Qiong XiaoDepartment of Agricultural, Food and Nutritional Science, University of Alberta, Edmonton, AB T6G 2P5, Canada.ORCID 0000-0001-8413-4425
Daniel BustosLaboratorio de Bioinformática y Química Computacional, Departamento de Medicina Traslacional, Facultad de Medicina, Universidad Católica Del Maule, Talca 3480094, Chile.ORCID 0000-0002-2136-2305
Kristian M CaldoDepartment of Sciences, Ambrose University, Calgary, AB T3H 0L5, Canada.
Luis Morales-QuintanaMultidisciplinary Agroindustry Research Laboratory, Instituto de Ciencias Biomédicas, Facultad de Ciencias de La Salud, Universidad Autónoma de Chile, Cinco Poniente #1670, Talca, Región del Maule 7500912, Chile.ORCID 0000-0002-7194-1989
Tao HuanDepartment of Chemistry, University of British Columbia, Vancouver, BC V6T 1Z1, Canada.ORCID 0000-0001-6295-2435
Guanqun ChenDepartment of Agricultural, Food and Nutritional Science, University of Alberta, Edmonton, AB T6G 2P5, Canada.ORCID 0000-0001-5790-3903

Funding

Canada Foundation for Innovation-John R. Evans Leaders Fund 41867Canada Research ChairsDiscovery GrantNatural Sciences and Engineering Research Council of CanadaResearch Capacity Program of Alberta RCP-22-023-SEG
6 · The paper itself

Abstract

Phosphatidylcholine (PC) is a crucial membrane phospholipid involved in both cellular processes and stress responses. CTP:phosphocholine cytidylyltransferase 1 (CCT1) is considered to catalyze a key regulatory step in primary PC de novo biosynthesis, but its functions and regulation are yet to be well elucidated. This study explored the physiological functions of CCT1 in Arabidopsis (Arabidopsis thaliana) (AthCCT1) in PC biosynthesis under normal growth conditions and in root development under osmotic stress, as well as its regulation by phosphorylation. Arabidopsis cct1 knockdown cct2 knockout lines exhibited significantly decreased PC intensities under normal growth conditions and impaired root growth under osmotic stress, which was rescued by AthCCT1 overexpression. Moreover, based on our previous findings that AthCCT1 is phosphorylated at Serine 187 (S187), we further investigated how this phosphorylation affects its biochemical and biological functions. The S187D phosphomimetic protein mutant of AthCCT1 exhibited reduced lipid-induced conformational changes and decreased enzymatic activity compared to the native protein. Molecular dynamics simulations of the S187D protein mutant revealed that the auto-inhibitory region, a conserved regulatory domain across CCT enzymes, remained closer to the αE helix, maintaining a constrained interaction between them. Consistent with the results of the in vitro analyses, overexpression of AthCCT1-S187D did not rescue stress-induced short-root phenotypes in cct1 knockdown cct2 knockout Arabidopsis lines. Taken together, the results revealed that AthCCT1 regulates PC biosynthesis under normal conditions and root development under osmotic stress, with its phosphorylation state at S187 playing an important role in modulating its enzymatic activity and physiological functions.

Indexed as

ArabidopsisArabidopsis ProteinsCholine-Phosphate CytidylyltransferasePhosphatidylcholinesPlant RootsGene Expression Regulation, PlantOsmotic PressurePhosphorylationArabidopsis ProteinsCholine-Phosphate CytidylyltransferasePhosphatidylcholines

Identifiers

PMID40561507
PMCPMC12238541

What Socratic holds

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LicenceCC BY-NC-ND
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Registered trials

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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 Socratic graph.