Evidence map›Paper›PMID 28366644›Full record

ArticleMolecular cell2017

A Metabolic Function for Phospholipid and Histone Methylation.

Cunqi Ye, Benjamin M Sutter, Yun Wang, Zheng Kuang, Benjamin P Tu

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 161 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
161citing papers in PubMed, 2 pooled it
10.0field-weighted citation impact, top 1% 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

161 citing papers in PubMed, 2 syntheses or guidelines pooled it, 263 citations in OpenAlex.

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101 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 1 institution in 1 country.

Cunqi YeDepartment of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9038, USA.
Benjamin M SutterDepartment of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9038, USA.
Yun WangDepartment of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9038, USA.
Zheng KuangDepartment of Immunology, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9038, USA.
Benjamin P TuDepartment of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9038, USA. Electronic address: benjamin.tu@utsouthwestern.edu.
The University of Texas Southwestern Medical Center · US

Funding

UT Southwestern Medical Center Simmons Comprehensive Cancer CenterP30CA142543 · NCI · UT SOUTHWESTERN MEDICAL CENTER · PI MELANIE H. COBB · 2010 to 2026
$53.7M
METABOLIC SIGNALS DRIVING CELL GROWTH & PROLIFERATIONR01GM094314 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI TU, BENJAMIN P · 2010 to 2019
$3.2M
NCI NIH HHS P30 CA142543NIGMS NIH HHS R01 GM094314
6 · The paper itself

Abstract

S-adenosylmethionine (SAM) is the methyl donor for biological methylation modifications that regulate protein and nucleic acid functions. Here, we show that methylation of a phospholipid, phosphatidylethanolamine (PE), is a major consumer of SAM. The induction of phospholipid biosynthetic genes is accompanied by induction of the enzyme that hydrolyzes S-adenosylhomocysteine (SAH), a product and inhibitor of methyltransferases. Beyond its function for the synthesis of phosphatidylcholine (PC), the methylation of PE facilitates the turnover of SAM for the synthesis of cysteine and glutathione through transsulfuration. Strikingly, cells that lack PE methylation accumulate SAM, which leads to hypermethylation of histones and the major phosphatase PP2A, dependency on cysteine, and sensitivity to oxidative stress. Without PE methylation, particular sites on histones then become methyl sinks to enable the conversion of SAM to SAH. These findings reveal an unforeseen metabolic function for phospholipid and histone methylation intrinsic to the life of a cell.

Indexed as

Protein Processing, Post-TranslationalCysteineEnergy MetabolismGene Expression ProfilingGene Expression Regulation, EnzymologicGene Expression Regulation, FungalHistonesLysineMethylationMutationOxidative StressPhosphatidylcholinesPhosphatidylethanolamine N-MethyltransferasePhosphatidylethanolaminesProtein Phosphatase 2Saccharomyces cerevisiaeCHO2 protein, S cerevisiaeCysteineHistonesLysinePhosphatidylcholinesphosphatidylethanolaminePhosphatidylethanolamine N-MethyltransferasePhosphatidylethanolaminesProtein Phosphatase 2Saccharomyces cerevisiae ProteinsS-AdenosylhomocysteineS-AdenosylmethioninecysteineepigeneticsglutathioneH3K36histone methylationmethyltransferasephospholipidsS-adenosylmethioninetranssulfuration

Identifiers

PMID28366644
PMCPMC5482412
OpenAlexW2601547636

What OpenQuestion holds

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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.