ArticleGlycobiology2017
Revisiting the human polypeptide GalNAc-T1 and T13 paralogs.
Article in Glycobiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 17 citations in OpenAlex.
- Decoding the complex substrate specificities of GalNAc-Ts.Glycobiology · 2025Review
- Carbohydrate-active enzyme (CAZyme) discovery and engineeringRSC chemical biology · 2024Review
- An unusual dual sugar-binding lectin domain controls the substrate specificity of a mucin-type O-glycosyltransferase.Science advances · 2024Article
- ISOGlyP: O-Glycosylation Site Prediction Using Peptide Sequences and GALNTs.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Role of TruncatedCancers · 2023Review
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- Article
- ISOGlyP: de novo prediction of isoform-specific mucin-type O-glycosylation.Glycobiology · 2021Article
- Glycans and Glycan-Binding Proteins as Regulators and Potential Targets in Leukocyte Recruitment.Frontiers in cell and developmental biology · 2021Review
- Differential splicing of the lectin domain of anThe Journal of biological chemistry · 2020Article
- Predicting mucin-type O-Glycosylation using enhancement value products from derived protein features.Journal of theoretical & computational chemistry · 2020Article
- Exploring Regulation of Protein O-Glycosylation in Isogenic Human HEK293 Cells by Differential O-Glycoproteomics.Molecular & cellular proteomics : MCP · 2019Article
- Polypeptide GalNAc-Ts: from redundancy to specificity.Current opinion in structural biology · 2019Review
Corrections and comments
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Authors and funding
15 authors at 5 institutions in 4 countries.
Funding
Abstract
Polypeptide GalNAc-transferases (GalNAc-Ts) constitute a family of 20 human glycosyltransferases (comprising 9 subfamilies), which initiate mucin-type O-glycosylation. The O-glycoproteome is thought to be differentially regulated via the different substrate specificities and expression patterns of each GalNAc-T isoforms. Here, we present a comprehensive in vitro analysis of the peptide substrate specificity of GalNAc-T13, showing that it essentially overlaps with the ubiquitous expressed GalNAc-T1 isoform found in the same subfamily as T13. We have also identified and partially characterized nine splice variants of GalNAc-T13, which add further complexity to the GalNAc-T family. Two variants with changes in their lectin domains were characterized by in vitro glycosylation assays, and one (Δ39Ex9) was inactive while the second one (Ex10b) had essentially unaltered activity. We used reverse transcription-polymerase chain reaction analysis of human neuroblastoma cell lines, normal brain and a small panel of neuroblastoma tumors to demonstrate that several splice variants (Ex10b, ΔEx9, ΔEx2-7 and ΔEx6/8-39bpEx9) were highly expressed in tumor cell lines compared with normal brain, although the functional implications remain to be unveiled. In summary, the GalNAc-T13 isoform is predicted to function similarly to GalNAc-T1 against peptide substrates in vivo, in contrast to a prior report, but is unique by being selectively expressed in the brain.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.