Evidence map›Paper›PMID 41812880›Full record

ArticleThe Journal of biological chemistry2026

Structural basis of EGF-repeat O-glucosylation by the protein O-glucosyltransferase POGLUT2.

Yuying Xia, Xinlin Hu, Zhengkang Hua, Min Zhang, Xuyang Ding, Yunshu Shi, Yan Ke, Jiameng Li, Hongjun Yu

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in
0citing papers in PubMed
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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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Yuying XiaDepartment of Biochemistry and Molecular Biology, School of Basic Medicine, Tongji Medical College and State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases and Hubei Key Laboratory of Natural Active Polysaccharides, Huazhong University of Science and Technology, Wuhan, China; Department of Pathogen Biology, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, China.
Xinlin HuDepartment of Pathogen Biology, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, China.
Zhengkang HuaDepartment of Biochemistry and Molecular Biology, School of Basic Medicine, Tongji Medical College and State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases and Hubei Key Laboratory of Natural Active Polysaccharides, Huazhong University of Science and Technology, Wuhan, China.
Min ZhangDepartment of Pathogen Biology, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, China.
Xuyang DingDepartment of Biochemistry and Molecular Biology, School of Basic Medicine, Tongji Medical College and State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases and Hubei Key Laboratory of Natural Active Polysaccharides, Huazhong University of Science and Technology, Wuhan, China.
Yunshu ShiDepartment of Biochemistry and Molecular Biology, School of Basic Medicine, Tongji Medical College and State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases and Hubei Key Laboratory of Natural Active Polysaccharides, Huazhong University of Science and Technology, Wuhan, China.
Yan KeDepartment of Biochemistry and Molecular Biology, School of Basic Medicine, Tongji Medical College and State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases and Hubei Key Laboratory of Natural Active Polysaccharides, Huazhong University of Science and Technology, Wuhan, China.
Jiameng LiDepartment of Biochemistry and Molecular Biology, School of Basic Medicine, Tongji Medical College and State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases and Hubei Key Laboratory of Natural Active Polysaccharides, Huazhong University of Science and Technology, Wuhan, China.
Hongjun YuDepartment of Biochemistry and Molecular Biology, School of Basic Medicine, Tongji Medical College and State Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases and Hubei Key Laboratory of Natural Active Polysaccharides, Huazhong University of Science and Technology, Wuhan, China; Cell Architecture Research Center, Huazhong University of Science and Technology, Wuhan, China. Electronic address: hongjun_yu@hust.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human protein O-glucosyltransferase 2 (POGLUT2) catalyzes the O-glucosylation of Notch receptors and extracellular matrix proteins, with its dysfunction linked to human disorders. Despite its physiological importance, the structural and mechanistic basis of POGLUT2 has remained elusive. Here, we report the first 1.79 Å structure of POGLUT2 in complex with UDP, revealing a three-domain architecture stabilized by an N-terminal filamin domain, which is unique in Notch-modifying enzymes. Integrated structural, computational, and functional analyses demonstrate that POGLUT2 recognizes structural features within epidermal growth factor-like repeats, including a conserved hydrophobic patch, which explains its stringent substrate selectivity. Our findings further identify Asp238 as the catalytic base, supporting an S

Indexed as

Epidermal Growth FactorGlucosyltransferasesGlycosylationHumansModels, MolecularEpidermal Growth FactorGlucosyltransferasesPOGLUT1 protein, humancrystal structuredisease mutationsEGF-repeatNotch signalingO-glucosylationPOGLUT2substrate recognition

Identifiers

PMID41812880
PMCPMC13084666

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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.