ArticleThe Journal of biological chemistry2009
Glycopeptide-preferring polypeptide GalNAc transferase 10 (ppGalNAc T10), involved in mucin-type O-glycosylation, has a unique GalNAc-O-Ser/Thr-binding site in its catalytic domain not found in ppGalNAc T1 or T2.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers, 1 of them a synthesis that pooled it.
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Who cites it
36 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Genome-wide association analyses for meat quality traits in Chinese Erhualian pigs and a Western Duroc × (Landrace × Yorkshire) commercial population.Genetics, selection, evolution : GSE · 2015Pooled it
- Decoding the complex substrate specificities of GalNAc-Ts.Glycobiology · 2025Review
- Carbohydrate-active enzyme (CAZyme) discovery and engineeringRSC chemical biology · 2024Review
- ISOGlyP: O-Glycosylation Site Prediction Using Peptide Sequences and GALNTs.Methods in molecular biology (Clifton, N.J.) · 2024Article
- The expression of O-linked glycosyltransferase GALNT7 in breast cancer is dependent on estrogen-, progesterone-, and HER2-receptor status, with prognostic implications.Glycoconjugate journal · 2023Article
- Polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) isozyme surface charge governs charge substrate preferences to modulate mucin type O-glycosylation.Glycobiology · 2023Article
- The effect of a methyl group on structure and function: Serine vs. threonine glycosylation and phosphorylation.Frontiers in molecular biosciences · 2023Review
- ISOGlyP: de novo prediction of isoform-specific mucin-type O-glycosylation.Glycobiology · 2021Article
- Structural basis for peptide substrate specificities of glycosyltransferase GalNAc-T2.ACS catalysis · 2021Article
- Article
- The Role of APPBiomolecules · 2020Review
- Engineering Orthogonal Polypeptide GalNAc-Transferase and UDP-Sugar Pairs.Journal of the American Chemical Society · 2019Article
- Exploring Regulation of Protein O-Glycosylation in Isogenic Human HEK293 Cells by Differential O-Glycoproteomics.Molecular & cellular proteomics : MCP · 2019Article
- IgA1 hinge-region clustered glycan fidelity is established early during semi-ordered glycosylation by GalNAc-T2.Glycobiology · 2019Article
- Polypeptide GalNAc-Ts: from redundancy to specificity.Current opinion in structural biology · 2019Review
- Structural and Mechanistic Insights into the Catalytic-Domain-Mediated Short-Range Glycosylation Preferences of GalNAc-T4.ACS central science · 2018Article
- EFEMP2 Mediates GALNT14-Dependent Breast Cancer Cell Invasion.Translational oncology · 2018Article
- Population differentiation in allele frequencies of obesity-associated SNPs.BMC genomics · 2017Article
- Article
- Revisiting the human polypeptide GalNAc-T1 and T13 paralogs.Glycobiology · 2017Article
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8 authors.
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Abstract
Mucin-type O-gly co sy la tion is initiated by a large family of UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferases (ppGalNAc Ts) that transfer GalNAc from UDP-GalNAc to the Ser and Thr residues of polypeptide acceptors. Some members of the family prefer previously gly co sylated peptides (ppGalNAc T7 and T10), whereas others are inhibited by neighboring gly co sy la tion (ppGalNAc T1 and T2). Characterizing their peptide and glycopeptide substrate specificity is critical for understanding the biological role and significance of each isoform. Utilizing a series of random peptide and glycopeptide substrates, we have obtained the peptide and glycopeptide specificities of ppGalNAc T10 for comparison with ppGalNAc T1 and T2. For the glycopeptide substrates, ppGalNAc T10 exhibited a single large preference for Ser/Thr-O-GalNAc at the +1 (C-terminal) position relative to the Ser or Thr acceptor site. ppGalNAc T1 and T2 revealed no significant enhancements suggesting Ser/Thr-O-GalNAc was inhibitory at most positions for these isoforms. Against random peptide substrates, ppGalNAc T10 revealed no significant hydrophobic or hydrophilic residue enhancements, in contrast to what has been reported previously for ppGalNAc T1 and T2. Our results reveal that these transferases have unique peptide and glycopeptide preferences demonstrating their substrate diversity and their likely roles ranging from initiating transferases to filling-in transferases.
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