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<p>The mouse is a key model in biomedical research, yet its tissue-specific glycoproteome remains incompletely characterized due to glycan complexity and microheterogeneity. Here, we present a comprehensive <i>N</i>-glycoproteomic atlas across 24 mouse tissues, comprising 3045 <i>N</i>-glycans with distinct structural features attached at 8681 glycosites on 74,277 glycopeptides and 5026 glycoproteins. Among these glycans, 2687 (88.2%) meet the high-confidence threshold through an integrative confidence-estimation framework. Overall glycan structural patterns show enormous tissue-specific diversities, acting as superior molecular signatures of tissue identity and system origins. Notably, even commonly expressed glycoproteins undergo tissue-dependent glycan remodeling, suggesting that glycosylation may fine-tune protein functions to meet specialized biological demands. These patterns are further shaped by subcellular localization, which constrains glycan variabilities across compartments. Co-occurrence network analyses also expose substructural biases and non-random microheterogeneities among glycans attached at the same glycosites. The dataset serves as a valuable database resource for advancing the structural and functional understanding of glycoproteins.</p>

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A comprehensive N-glycoproteome atlas reveals tissue-specific glycan remodeling but non-random structural microheterogeneities

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年1月13日

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  • Yongqi Wu,
  • Muyao Yang,
  • Yongchao Xu,
  • Li Jia,
  • Jun Li,
  • Xiaohan Wang,
  • Jiayu Zhao,
  • Yinli Cai,
  • Yiwen Zhang,
  • Shisheng Sun

摘要

The mouse is a key model in biomedical research, yet its tissue-specific glycoproteome remains incompletely characterized due to glycan complexity and microheterogeneity. Here, we present a comprehensive N-glycoproteomic atlas across 24 mouse tissues, comprising 3045 N-glycans with distinct structural features attached at 8681 glycosites on 74,277 glycopeptides and 5026 glycoproteins. Among these glycans, 2687 (88.2%) meet the high-confidence threshold through an integrative confidence-estimation framework. Overall glycan structural patterns show enormous tissue-specific diversities, acting as superior molecular signatures of tissue identity and system origins. Notably, even commonly expressed glycoproteins undergo tissue-dependent glycan remodeling, suggesting that glycosylation may fine-tune protein functions to meet specialized biological demands. These patterns are further shaped by subcellular localization, which constrains glycan variabilities across compartments. Co-occurrence network analyses also expose substructural biases and non-random microheterogeneities among glycans attached at the same glycosites. The dataset serves as a valuable database resource for advancing the structural and functional understanding of glycoproteins.