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March 1, 2026Journal of Biological ChemistryOpen Access

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

Ye Xia Xinlin Hu Zhengkang Hua M Zhang Xu Ding Yunshu Shi Yan Ke Jiameng Li Hongjun Yu

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Key Points

This research aims to elucidate the structural and mechanistic basis of POGLUT2 in EGF-repeat O-glucosylation.
Determined the 1.79 Å structure of POGLUT2 in complex with UDP.
Conducted integrated structural, computational, and functional analyses.
Identified key structural features and catalytic mechanisms.
Revealed a unique three-domain architecture of POGLUT2.
Found Asp238 to be the catalytic base for O-glucosylation.
Showed that cancer-associated mutations disrupt enzymatic activity and structural integrity.

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Implication

Structural analysis reveals POGLUT2's substrate selectivity in O-glucosylation, suggesting implications for human diseases.

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Cite This Study

Xia et al. (2026) studied this question.

synapsesocial.com/papers/69b2581996eeacc4fcec7606 https://doi.org/10.1016/j.jbc.2026.111361

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