Evidence map›Paper›PMID 40045035›Full record

ReviewCell death and differentiation2025

Crosstalk between O-GlcNAcylation and phosphorylation in metabolism: regulation and mechanism.

Qijie Zhao, Shisheng Zhou, Wenhui Lou, Hui Qian, Zhiwei Xu

Abstract readReview
In one paragraph

Review in Cell death and differentiation, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Review
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  11. Glycan-related genes and genetic disorders.Journal of human genetics · 2026
    Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Review
  18. Article
  19. Review
  20. Glycosylation in kidney diseases.Precision clinical medicine · 2025
    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

5 authors.

Qijie Zhao *Jiangsu Key Laboratory of Medical Science and Laboratory Medicine, Department of Laboratory Medicine, School of Medicine, Jiangsu University, Zhenjiang, Jiangsu, China.ORCID 0009-0002-0632-5706
Shisheng Zhou *Jiangsu Key Laboratory of Medical Science and Laboratory Medicine, Department of Laboratory Medicine, School of Medicine, Jiangsu University, Zhenjiang, Jiangsu, China.ORCID 0009-0003-6171-7830
Wenhui Lou *Jiangsu Key Laboratory of Medical Science and Laboratory Medicine, Department of Laboratory Medicine, School of Medicine, Jiangsu University, Zhenjiang, Jiangsu, China.ORCID 0009-0009-0989-4905
Hui QianJiangsu Key Laboratory of Medical Science and Laboratory Medicine, Department of Laboratory Medicine, School of Medicine, Jiangsu University, Zhenjiang, Jiangsu, China. lstmmmlst@163.com.ORCID 0000-0002-0098-3196
Zhiwei XuJiangsu Key Laboratory of Medical Science and Laboratory Medicine, Department of Laboratory Medicine, School of Medicine, Jiangsu University, Zhenjiang, Jiangsu, China. zhiweixu@ujs.edu.cn.ORCID 0000-0001-5768-0121

Funding

National Natural Science Foundation of China (National Science Foundation of China) No. 32000903
6 · The paper itself

Abstract

Cells produce metabolic intermediates through catalytic reactions, mainly via post-translational modifications. The modification of proteins by O-linked N-acetylglucosamine, known as O-GlcNAcylation, is one of the most common post-translational modifications. As O-GlcNAcylation and phosphorylation can occur at serine or threonine residues, it is crucial that the interplay between these two modifications is vital to bioenergetic and biosynthetic demand. Although emerging recognition linking O-GlcNAc modification and phosphorylation to protein functions has been obtained, the issue of how altered O-GlcNAcylation or phosphorylation regulates each other in the metabolic system remains uncertain. The combination of cell biological and proteomic approaches over the recent few years has not only highlighted the interactions between O-GlcNAcylation and phosphorylation in protein function but also prompted us to elucidate the underlying mechanisms behind this crosstalk controlling metabolic homeostasis. The purpose of this review is to summarize recent advances in the O-GlcNAcylation/phosphorylation regulation of the metabolic process. An extensive exploration of this interplay has significant implications for metabolic control systems, including glucose, lipid, and nucleotide metabolism, where dysregulation in O-GlcNAcylation and phosphorylation of metabolic syndrome is essential.

Indexed as

AcetylglucosamineProtein Processing, Post-TranslationalAnimalsGlycosylationHumansN-AcetylglucosaminyltransferasesPhosphorylationAcetylglucosamineN-Acetylglucosaminyltransferases

Identifiers

PMID40045035
PMCPMC12284140

What OpenQuestion holds

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Registered trials

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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.