包括的なN結合型糖タンパク質アトラスが組織特異的な糖鎖リモデリングと非ランダムな構造的微細不均一性を明らかにする
Yongqi Wu1, Muyao Yang1, Yongchao Xu1
1Laboratory for Disease Glycoproteomics, College of Life Sciences, Northwest University, Xi'an, PR China.
Abstract:
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.
関連する概念動画
Proteoglycans
Protein Glycosylation
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Oligosaccharide Assembly
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Matrix Proteoglycans and Glycoproteins


