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  3. A Reversible Chemoenzymatic Labeling Strategy for Profiling of Protein O-Glucosylation

A Reversible Chemoenzymatic Labeling Strategy for Profiling of Protein O-Glucosylation

  • Angew Chem Int Ed Engl. 2025 Oct 11:e202513638. doi: 10.1002/anie.202513638.
Shilin Zhang # 1 2 3,  Yinping Tian # 1 2,  Yuqiu Wang # 4,  Fangyu Wei 1 2 3,  Hu Zhou 4 3,  Liuqing Wen 1 2 3
Affiliations

Affiliations

  • 1 State Key Laboratory of Chemical Biology, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, 201203, China.
  • 2 Carbohydrate-Based Drug Research Center, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, 201203, China.
  • 3 University of Chinese Academy of Sciences, Beijing, 100049, China.
  • 4 Department of Analytical Chemistry, State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, 201203, China.
  • # Contributed equally.
PMID: 41074817 DOI: 10.1002/anie.202513638
Abstract

O-linked glucose (O-Glc), the β-linked modification of serine residues, is a rare form of protein glycosylation first identified on proteins containing epidermal growth factor (EGF)-like domains (canonical O-Glc). Several recent studies revealed that proteins lacking EGF-like domains could also undergo O-Glc modification (noncanonical O-Glc). However, the biosynthetic origin and biological function of protein O-glucosylation remain poorly understood and debated, owing to the lack of effective analytical tools. Here, a reversible chemoenzymatic labeling strategy for O-Glc analysis is described. By the strategy described, a large number of canonical and noncanonical O-Glc sites were identified in human cell lines, indicating that protein O-Glc is a widespread post-translational protein modification.

Keywords

Chemoenzymatic labeling; Endoglycosidase; Glycoproteomic; O‐Glc; Protein glycosylation.

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