Evidence map›Paper›PMID 25293755›Full record

ArticleThe Plant cell2014

Arabidopsis lipins, PDAT1 acyltransferase, and SDP1 triacylglycerol lipase synergistically direct fatty acids toward β-oxidation, thereby maintaining membrane lipid homeostasis.

Jilian Fan, Chengshi Yan, Rebecca Roston, John Shanklin, Changcheng Xu

Open access · greenAbstract read
In one paragraph

Article in The Plant cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed, 1 pooled it
7.4field-weighted citation impact, top 3% 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

87 citing papers in PubMed, 1 synthesis or guideline pooled it, 169 citations in OpenAlex.

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Jilian FanBioscience Department, Brookhaven National Laboratory, Upton, New York 11973.
Chengshi YanBioscience Department, Brookhaven National Laboratory, Upton, New York 11973.
Rebecca RostonDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan 48824.
John ShanklinBioscience Department, Brookhaven National Laboratory, Upton, New York 11973.
Changcheng XuBioscience Department, Brookhaven National Laboratory, Upton, New York 11973 cxu@bnl.gov.ORCID http://orcid.org/0000-0002-0179-9462
Brookhaven National Laboratory · USMichigan State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Triacylglycerol (TAG) metabolism is a key aspect of intracellular lipid homeostasis in yeast and mammals, but its role in vegetative tissues of plants remains poorly defined. We previously reported that PHOSPHOLIPID:DIACYLGLYCEROL ACYLTRANSFERASE1 (PDAT1) is crucial for diverting fatty acids (FAs) from membrane lipid synthesis to TAG and thereby protecting against FA-induced cell death in leaves. Here, we show that overexpression of PDAT1 enhances the turnover of FAs in leaf lipids. Using the trigalactosyldiacylglycerol1-1 (tgd1-1) mutant, which displays substantially enhanced PDAT1-mediated TAG synthesis, we demonstrate that disruption of SUGAR-DEPENDENT1 (SDP1) TAG lipase or PEROXISOMAL TRANSPORTER1 (PXA1) severely decreases FA turnover, leading to increases in leaf TAG accumulation, to 9% of dry weight, and in total leaf lipid, by 3-fold. The membrane lipid composition of tgd1-1 sdp1-4 and tgd1-1 pxa1-2 double mutants is altered, and their growth and development are compromised. We also show that two Arabidopsis thaliana lipin homologs provide most of the diacylglycerol for TAG synthesis and that loss of their functions markedly reduces TAG content, but with only minor impact on eukaryotic galactolipid synthesis. Collectively, these results show that Arabidopsis lipins, along with PDAT1 and SDP1, function synergistically in directing FAs toward peroxisomal β-oxidation via TAG intermediates, thereby maintaining membrane lipid homeostasis in leaves.

Indexed as

HomeostasisAcyltransferasesAdenosine TriphosphatasesArabidopsisArabidopsis ProteinsATP-Binding Cassette Transportersbeta-GlucosidaseCarboxylic Ester HydrolasesFatty AcidsGene Expression Regulation, PlantLipaseLipid DropletsMembrane LipidsMembrane Transport ProteinsMicroscopy, Electron, TransmissionMicroscopy, FluorescenceAcyltransferasesAdenosine TriphosphatasesArabidopsis ProteinsAt4g39850 protein, ArabidopsisATP-Binding Cassette Transportersbeta-GlucosidaseCarboxylic Ester HydrolasesFatty AcidsLipaseMembrane LipidsMembrane Transport ProteinsPDAT1 protein, ArabidopsisSDP1 protein, ArabidopsisSFR2 protein, ArabidopsisTGD1 protein, ArabidopsisTriglycerides

Identifiers

PMID25293755
PMCPMC4247580
OpenAlexW2011876677

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.