Evidence map›Paper›PMID 29524020›Full record

ArticleJournal of bioenergetics and biomembranes2018

Cross regulation between mTOR signaling and O-GlcNAcylation.

Ninon Very, Agata Steenackers, Caroline Dubuquoy, Jeanne Vermuse, Laurent Dubuquoy, Tony Lefebvre, Ikram El Yazidi-Belkoura

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of bioenergetics and biomembranes, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

35 citing papers in PubMed, 47 citations in OpenAlex.

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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

7 authors at 5 institutions in 2 countries.

Ninon VeryCNRS, UMR 8576 - UGSF - Unité de Glycobiologie Structurale et Fonctionnelle, Université de Lille, F 59000, Lille, France.
Agata SteenackersLaboratory of Cell Biochemistry and Biology, NIDDK, National Institutes of Health, Bethesda, MD, USA.
Caroline DubuquoyINSERM, U995, LIRIC - Lille Inflammation Research International Center, CHU Lille, Université de Lille, F 59000, Lille, France.
Jeanne VermuseCNRS, UMR 8576 - UGSF - Unité de Glycobiologie Structurale et Fonctionnelle, Université de Lille, F 59000, Lille, France.
Laurent DubuquoyINSERM, U995, LIRIC - Lille Inflammation Research International Center, CHU Lille, Université de Lille, F 59000, Lille, France.
Tony LefebvreCNRS, UMR 8576 - UGSF - Unité de Glycobiologie Structurale et Fonctionnelle, Université de Lille, F 59000, Lille, France.
Ikram El Yazidi-BelkouraCNRS, UMR 8576 - UGSF - Unité de Glycobiologie Structurale et Fonctionnelle, Université de Lille, F 59000, Lille, France. ikram.el-yazidi@univ-lille1.fr.
Lille Inflammation Research International Center · FRUniversité de Lille · FRCentre National de la Recherche Scientifique · FRNational Institute of Diabetes and Digestive and Kidney Diseases · USUnité de Glycobiologie Structurale et Fonctionnelle · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The hexosamine biosynthetic pathway (HBP) integrates glucose, amino acids, fatty acids and nucleotides metabolisms for uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis. UDP-GlcNAc is the nucleotide sugar donor for O-linked β-N-acetylglucosaminylation (O-GlcNAcylation) processes. O-GlcNAc transferase (OGT) is the enzyme which transfers the N-acetylglucosamine (O-GlcNAc) residue onto target proteins. Several studies previously showed that glucose metabolism dysregulations associated with obesity, diabetes or cancer correlated with an increase of OGT expression and global O-GlcNAcylation levels. Moreover, these diseases present an increased activation of the nutrient sensing mammalian target of rapamycin (mTOR) pathway. Other works demonstrate that mTOR regulates protein O-GlcNAcylation in cancer cells through stabilization of OGT. In this context, we studied the cross-talk between these two metabolic sensors in vivo in obese mice predisposed to diabetes and in vitro in normal and colon cancer cells. We report that levels of OGT and O-GlcNAcylation are increased in obese mice colon tissues and colon cancer cells and are associated with a higher activation of mTOR signaling. In parallel, treatments with mTOR regulators modulate OGT and O-GlcNAcylation levels in both normal and colon cancer cells. However, deregulation of O-GlcNAcylation affects mTOR signaling activation only in cancer cells. Thus, a crosstalk exists between O-GlcNAcylation and mTOR signaling in contexts of metabolism dysregulation associated to obesity or cancer.

Indexed as

Signal TransductionAcetylglucosamineAnimalsColonic NeoplasmsGlycosylationMiceMice, ObeseN-AcetylglucosaminyltransferasesObesityReceptor Cross-TalkTOR Serine-Threonine KinasesAcetylglucosaminemTOR protein, mouseN-AcetylglucosaminyltransferasesO-GlcNAc transferaseTOR Serine-Threonine KinasesCancerColonMetabolismmTOR signalingObesityO-GlcNAcylation

Identifiers

PMID29524020
OpenAlexW2790027144

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.