Evidence map›Paper›PMID 40670355›Full record

ArticleNature communications2025

Human glycogenins maintain glucose homeostasis by regulating glycogen metabolism.

Tzu-Han Weng, Yu-Chung Pien, Ching-Jou Chen, Po-Pang Chen, Yu-Ting Tseng, Ying-Chen Chen, Wen-Po Hsiao, Ying-Ting Lee, Yi-An Chen, Yao-Chi Chen and 6 more

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
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

16 authors.

Tzu-Han WengDepartment of Life Science, National Taiwan University, Taipei, Taiwan.
Yu-Chung Pien *Department of Life Science, National Taiwan University, Taipei, Taiwan.ORCID http://orcid.org/0000-0001-6028-2044
Ching-Jou Chen *Department of Life Science, National Taiwan University, Taipei, Taiwan.
Po-Pang Chen *Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan.ORCID http://orcid.org/0009-0001-8533-301X
Yu-Ting TsengInstitute of Molecular Biology, Academia Sinica, Taipei, Taiwan.
Ying-Chen ChenDepartment of Life Science, National Taiwan University, Taipei, Taiwan.
Wen-Po HsiaoDepartment of Life Science, National Taiwan University, Taipei, Taiwan.
Ying-Ting LeeDepartment of Life Science, National Taiwan University, Taipei, Taiwan.
Yi-An ChenInstitute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.
Yao-Chi ChenInstitute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan.
Carmay LimInstitute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan.ORCID http://orcid.org/0000-0001-9077-7769
Tzu-Han HsuInstitute of Molecular Biology, Academia Sinica, Taipei, Taiwan.
Sung-Jan LinDepartment of Biomedical Engineering, College of Medicine and College of Engineering, National Taiwan University, Taipei, Taiwan.ORCID http://orcid.org/0000-0003-1325-3464
Hsin-Yung YenInstitute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.ORCID http://orcid.org/0000-0002-6612-3324
Kuo-Chiang HsiaInstitute of Molecular Biology, Academia Sinica, Taipei, Taiwan. khsia@gate.sinica.edu.tw.ORCID http://orcid.org/0000-0002-4409-6732
Su-Yi TsaiDepartment of Life Science, National Taiwan University, Taipei, Taiwan. suyitsai@ntu.edu.tw.ORCID http://orcid.org/0000-0002-7423-645X

Funding

National Taiwan University (NTU) 112L895405National Taiwan University (NTU) 113L893105
6 · The paper itself

Abstract

Proper regulation of glycogen metabolism is fundamental to cellular energy homeostasis, and its disruption is associated with various metabolic disorders, including glycogen storage diseases (GSDs) and potentially diabetes. Despite glycogen's role as an essential energy reservoir, the mechanisms governing its synthesis and structural diversity across tissues remain unclear. Here, we uncover the distinct physiological roles of the human glycogenins GYG1 and GYG2 in glycogen synthesis. Through cellular models, structural biology, and biochemical analyses, we demonstrate that, unlike GYG1, GYG2 exhibits minimal autoglycosylation activity and acts as a suppressor of glycogen formation. Together, these two glycogenins coordinate glycogen synthase activity and influence glycogen assembly in a cell-type-dependent manner. Importantly, these glycogenins modulate glucose metabolic pathways, thereby ensuring cellular glucose homeostasis. These findings address longstanding questions in glycogen metabolism and establish both GYG1 and GYG2 as critical regulators of glycogen synthesis and breakdown in human, providing insights with potential therapeutic implications for treating GSDs and metabolic diseases.

Indexed as

GlucoseGlucosyltransferasesGlycogenGlycoproteinsHomeostasisCell LineGlycosylationHuman Embryonic Stem CellsHumansModels, MolecularParticle SizePhosphorylationProtein BindingProtein Structure, QuaternaryProtein Structure, TertiaryGlucoseGlucosyltransferasesGlycogenglycogeninGlycoproteinsGYG2 protein, human

Identifiers

PMID40670355
PMCPMC12267440

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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.