ArticleThe Journal of biological chemistry2016
Extrinsic Functions of Lectin Domains in O-N-Acetylgalactosamine Glycan Biosynthesis.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 13 citations in OpenAlex.
- SLC10A7 regulates O-GalNAc glycosylation and CaCellular and molecular life sciences : CMLS · 2025Article
- O-glycosylation of IgA1 and the pathogenesis of an autoimmune disease IgA nephropathy.Glycobiology · 2024Review
- Polypeptide N-acetylgalactosamine transferase 3: a post-translational writer on human health.Journal of molecular medicine (Berlin, Germany) · 2022Review
- 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
- Biosynthesis ofThe Journal of biological chemistry · 2019Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glycan biosynthesis occurs mainly in Golgi. Molecular organization and functional regulation of this process are not well understood. We evaluated the extrinsic effect of lectin domains (β-trefoil fold) of polypeptide GalNAc-transferases (ppGalNAc-Ts) on catalytic activity of glycosyltransferases during O-GalNAc glycan biosynthesis. The presence of lectin domain T3lec or T4lec during ppGalNAc-T2 and ppGalNAc-T3 catalytic reaction had a clear inhibitory effect on GalNAc-T activity. Interaction of T3lec or T4lec with ppGalNAc-T2 catalytic domain was not mediated by carbohydrate. T3lec, but not T2lec and T4lec, had a clear activating effect on Drosophila melanogaster core 1 galactosyltransferase enzyme activity and a predominant inhibitory effect on in vivo human core 1 glycan biosynthesis. The regulatory role of the β-trefoil fold of ppGalNAc-Ts in enzymatic activity of glycosyltransferases involved in the O-glycan biosynthesis pathway, described here for the first time, helps clarify the mechanism of biosynthesis of complex biopolymers (such as glycans) that is not template-driven.
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Registered trials
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