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Primate-specific regulation of the human glycosphingolipid gatekeeper UGCG

Research Structural Biology

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TL;DR - Cryogenic electron microscopy structures reveal how full-length human UGCG, a key regulator of glycosphingolipid diversity, catalyses its reaction. The findings identify a metal-independent mechanism driven by an arginine network.

  • Reports cryo-EM structures of full-length human UGCG.
  • UGCG controls the scale and composition of glycosphingolipid diversity.
  • The structures indicate that catalysis does not require a metal cofactor.
  • An arginine network drives the proposed catalytic mechanism.

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Primate-specific regulation of the human glycosphingolipid gatekeeper UGCG

Nature Canrong Wu, Sanshan Jin, Jiuyin Xu, James Jiqi Wang, Xiaoqi Guo, Yunhai Li, Zhenyu Cao, Mengting Jiang, Qingning Yuan, Wen Hu, Changyao Li, Youwei Xu, Ming-Wei Wang, Yi Jiang, H. Eric Xu 2026-08-26 doi:10.1038/s41586-026-10927-4
Public signals OpenAlex citations 1 · Semantic Scholar citations 1 · Semantic Scholar influential citations 0
Providers: Hugging Face · N/A OpenAlex · Citations 1 Publisher · N/A Semantic Scholar · Citations 1 · Influential citations 0 X · N/A Fetched 2026-09-25 14:27:32.532204 UTC

TL;DR - Cryogenic electron microscopy structures reveal how full-length human UGCG, a key regulator of glycosphingolipid diversity, catalyses its reaction. The findings identify a metal-independent mechanism driven by an arginine network.

  • Reports cryo-EM structures of full-length human UGCG.
  • UGCG controls the scale and composition of glycosphingolipid diversity.
  • The structures indicate that catalysis does not require a metal cofactor.
  • An arginine network drives the proposed catalytic mechanism.
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