Evidence map›Paper›PMID 40571812›Full record

ArticleScience China. Life sciences2025

ULK1-dependent phosphorylation of OGT instructs the tumorigenicity of O-GlcNAcylation.

Zhuan Lv, Qingen Da, Yumiao Li, Aiyun Yuan, Guangcan Shao, Xiaoxuan Lu, Yue Wang, Xuefang Zhang, Jingjing Liu, Meng-Qiu Dong and 4 more

Abstract read
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In one paragraph

Article in Science China. Life sciences, 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. Review
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

14 authors.

Zhuan Lv *Beijing Key Laboratory of DNA Damage Response and College of Life Sciences, Capital Normal University, Beijing, 100048, China.
Qingen Da *Department of Cardiovascular Surgery, Peking University Shenzhen Hospital, Shenzhen, 518036, China.
Yumiao Li *College of Life Sciences, Hebei University, Baoding, 071002, China.
Aiyun Yuan *Beijing Key Laboratory of DNA Damage Response and College of Life Sciences, Capital Normal University, Beijing, 100048, China.
Guangcan ShaoNational Institute of Biological Sciences, Beijing, 102206, China.
Xiaoxuan LuBeijing Key Laboratory of DNA Damage Response and College of Life Sciences, Capital Normal University, Beijing, 100048, China.
Yue WangState Key Laboratory of Natural and Biomimetic Drugs, School of Pharmaceutical Sciences, Peking University, Beijing, 100191, China.
Xuefang ZhangCollege of Life Sciences, Hebei University, Baoding, 071002, China.
Jingjing LiuDepartment of Cardiovascular Surgery, Peking University Shenzhen Hospital, Shenzhen, 518036, China.
Meng-Qiu DongNational Institute of Biological Sciences, Beijing, 102206, China.
Yuanyuan RuanKey Laboratory of Glycoconjugate Research Ministry of Health, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Fudan University, Shanghai, 200032, China. yuanyuanruan@fudan.edu.cn.
Chen WuCollege of Life Sciences, Hebei University, Baoding, 071002, China. wuchen@hbu.edu.cn.
Kunfu OuyangDepartment of Cardiovascular Surgery, Peking University Shenzhen Hospital, Shenzhen, 518036, China. ouyang_kunfu@pku.edu.cn.
Jing LiBeijing Key Laboratory of DNA Damage Response and College of Life Sciences, Capital Normal University, Beijing, 100048, China. jing_li@mail.cnu.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Investigations from the last four decades have correlated high O-linked N-acetylglucosamine (O-GlcNAc) levels with various cancer types, but it is not known how OGT responds to diverse nutrients to finetune cellular O-GlcNAcylation levels. Herein we identified a critical OGT phosphorylation site by unc-51 like autophagy activating kinase 1 (ULK1) under glucose depletion. First, we demonstrated that glucose levels modulate the interaction between OGT and ULK1 and cellular O-GlcNAcylation levels. Low glucose induces high O-GlcNAcylation, which could be reversed by ULK1 inhibition. Then, using mass spectrometry, we showed that ULK1 phosphorylates OGT at Ser576 and stabilizes OGT. Further biochemical experiments revealed that Ser576 phosphorylation inhibits Lys604 ubiquitination by stimulating OGT binding with BAP1, a de-ubiquitinase for OGT. Strikingly, using the OGT

Indexed as

AcetylglucosamineAutophagy-Related Protein-1 HomologCarcinogenesisIntracellular Signaling Peptides and ProteinsN-AcetylglucosaminyltransferasesAnimalsCell Line, TumorGlucoseGlycosylationHEK293 CellsHumansMiceMice, NudePhosphorylationUbiquitinationAcetylglucosamineAutophagy-Related Protein-1 HomologGlucoseIntracellular Signaling Peptides and ProteinsN-AcetylglucosaminyltransferasesOGT protein, humanULK1 protein, humanBAP1glucoseO-GlcNAcylationO-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT)ULK1

Identifiers

PMID40571812

What OpenQuestion holds

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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 OpenQuestion graph.