Evidence map›Paper›PMID 31911580›Full record

ArticleNature communications2020

O-GlcNAcylation of PGK1 coordinates glycolysis and TCA cycle to promote tumor growth.

Hao Nie, Haixing Ju, Jiayi Fan, Xiaoliu Shi, Yaxian Cheng, Xiaohui Cang, Zhiguo Zheng, Xiaotao Duan, Wen Yi

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 208 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
208citing papers in PubMed, 1 pooled it
14.1field-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

208 citing papers in PubMed, 1 synthesis or guideline pooled it, 340 citations in OpenAlex.

  1. Pooled it
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  8. PGK1 Suppresses CD8Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
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148 more citing papers are in PubMed but not listed here.

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

9 authors at 3 institutions in 1 country.

Hao NieMOE Key Laboratory of Biosystems Homeostasis & Protection, College of Life Sciences; The First Affiliated Hospital, School of Medicine, Zhejiang University, 310058, Hangzhou, China.
Haixing JuDepartment of Colorectal Surgery, Zhejiang Cancer Hospital, 310022, Hangzhou, China.
Jiayi FanMOE Key Laboratory of Biosystems Homeostasis & Protection, College of Life Sciences; The First Affiliated Hospital, School of Medicine, Zhejiang University, 310058, Hangzhou, China.
Xiaoliu ShiMOE Key Laboratory of Biosystems Homeostasis & Protection, College of Life Sciences; The First Affiliated Hospital, School of Medicine, Zhejiang University, 310058, Hangzhou, China.
Yaxian ChengMOE Key Laboratory of Biosystems Homeostasis & Protection, College of Life Sciences; The First Affiliated Hospital, School of Medicine, Zhejiang University, 310058, Hangzhou, China.
Xiaohui CangDivision of Medical Genetics and Genomics, The Children's Hospital, School of Medicine, Zhejiang University, 310058, Hangzhou, China.
Zhiguo ZhengDepartment of Colorectal Surgery, Zhejiang Cancer Hospital, 310022, Hangzhou, China.
Xiaotao DuanState Key Laboratory of Toxicology and Medical Countermeasures, Beijing Institute of Pharmacology and Toxicology, 100850, Beijing, China.
Wen YiMOE Key Laboratory of Biosystems Homeostasis & Protection, College of Life Sciences; The First Affiliated Hospital, School of Medicine, Zhejiang University, 310058, Hangzhou, China. wyi@zju.edu.cn.
Zhejiang University · CNZhejiang Cancer Hospital · CNChildren's Hospital of Zhejiang University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many cancer cells display enhanced glycolysis and suppressed mitochondrial metabolism. This phenomenon, known as the Warburg effect, is critical for tumor development. However, how cancer cells coordinate glucose metabolism through glycolysis and the mitochondrial tricarboxylic acid (TCA) cycle is largely unknown. We demonstrate here that phosphoglycerate kinase 1 (PGK1), the first ATP-producing enzyme in glycolysis, is reversibly and dynamically modified with O-linked N-acetylglucosamine (O-GlcNAc) at threonine 255 (T255). O-GlcNAcylation activates PGK1 activity to enhance lactate production, and simultaneously induces PGK1 translocation into mitochondria. Inside mitochondria, PGK1 acts as a kinase to inhibit pyruvate dehydrogenase (PDH) complex to reduce oxidative phosphorylation. Blocking T255 O-GlcNAcylation of PGK1 decreases colon cancer cell proliferation, suppresses glycolysis, enhances the TCA cycle, and inhibits tumor growth in xenograft models. Furthermore, PGK1 O-GlcNAcylation levels are elevated in human colon cancers. This study highlights O-GlcNAcylation as an important signal for coordinating glycolysis and the TCA cycle to promote tumorigenesis.

Indexed as

Citric Acid CycleGlycolysisAcetylglucosamineAmino Acid MotifsAnimalsCell Line, TumorColonic NeoplasmsHumansMaleMiceMice, NudeMitochondriaPhosphoglycerate KinasePyruvate Dehydrogenase ComplexAcetylglucosaminePGK1 protein, humanPhosphoglycerate KinasePyruvate Dehydrogenase Complex

Identifiers

PMID31911580
PMCPMC6946671
OpenAlexW2999943581

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.