ArticleGlycobiology2008
Conservation of peptide acceptor preferences between Drosophila and mammalian polypeptide-GalNAc transferase ortholog pairs.
Article in Glycobiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 54 citations in OpenAlex.
- A single catalytic domain residue regulates the substrate specificity of a mucin-type O-glycosyltransferase in salivary gland function.bioRxiv : the preprint server for biology · 2025Article
- Decoding the complex substrate specificities of GalNAc-Ts.Glycobiology · 2025Review
- Charge matters: how flanking substrate charge modulates O-glycan Core elongation.Glycobiology · 2025Article
- 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
- Polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) isozyme surface charge governs charge substrate preferences to modulate mucin type O-glycosylation.Glycobiology · 2023Article
- The role of glycoconjugates as receptors for insecticidal proteins.FEMS microbiology reviews · 2023Review
- The effect of a methyl group on structure and function: Serine vs. threonine glycosylation and phosphorylation.Frontiers in molecular biosciences · 2023Review
- In vivo models of mucin biosynthesis and function.Advanced drug delivery reviews · 2022Review
- 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
- Influence of theJournal of genetics · 2021Article
- The Role of APPBiomolecules · 2020Review
- Ser and Thr acceptor preferences of the GalNAc-Ts vary among isoenzymes to modulate mucin-type O-glycosylation.Glycobiology · 2020Article
- Predicting mucin-type O-Glycosylation using enhancement value products from derived protein features.Journal of theoretical & computational chemistry · 2020Article
- IgA1 hinge-region clustered glycan fidelity is established early during semi-ordered glycosylation by GalNAc-T2.Glycobiology · 2019Article
- Structural and Mechanistic Insights into the Catalytic-Domain-Mediated Short-Range Glycosylation Preferences of GalNAc-T4.ACS central science · 2018Article
- The Interaction of the Gut Microbiota with the Mucus Barrier in Health and Disease in Human.Microorganisms · 2018Review
- Eukaryotic protein glycosylation: a primer for histochemists and cell biologists.Histochemistry and cell biology · 2017Review
- Revisiting the human polypeptide GalNAc-T1 and T13 paralogs.Glycobiology · 2017Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltrans- ferases (ppGalNAc Ts) comprise a large family of glycosyltransferases that initiate mucin-type protein O-glycosylation, transferring alpha-GalNAc to Thr and Ser residues of polypeptide acceptors. Families of ppGalNAc Ts are found across diverse eukaryotes with orthologs identifiable from mammals to single-cell organisms. The peptide substrate specificity and specific protein targets of the individual ppGalNAc T family members remain poorly understood. Previously, we reported a series of oriented random peptide substrate libraries for quantitatively determining the peptide substrate specificities of the mammalian ppGalNAc T1 and T2 (Gerken TA, Raman J, Fritz TA, Jamison O. 2006. Identification of common and unique peptide substrate preferences for the UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferases T1 & T2 (ppGalNAc T1 & T2) derived from oriented random peptide substrates. J Biol Chem. 281:32403-32416). With these substrates, previously unknown features of the transferases were revealed. Utilizing these and a new lengthened set of random peptides, studies have now been performed on PGANT5 and PGANT2, the Drosophila orthologs of T1 and T2. The results from these studies suggest that the major peptide substrate determinants for these transferases are contained within 2 to 3 residues flanking the site of glycosylation. It is further found that the mammalian and fly T1 orthologs display very similar peptide substrate preferences, while the T2 orthologs are nearly indistinguishable, suggesting similar peptide preferences amongst orthologous pairs have been maintained across evolution. This conclusion is further supported by sequence homology comparisons of each of the transferase orthologs, showing that the peptide substrate and UDP binding site residues are more highly conserved between species relative to their remaining catalytic and lectin domain residues.
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Registered trials
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