Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 291, Issue 49, Pages 25339-25350Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M116.740795
Keywords
glycobiology; glycoprotein biosynthesis; glycosylation inhibitor; lectin; mucin
Categories
Funding
- Argentinean Institutions Consejo Nacional de Investigaciones Cientificas y Ticnicas
- Argentinean Institutions Consejo Nacional de Investigaciones Cientificas y Tecnicas
- Secretaria de Ciencia y Tecnologia (Universidad Nacional de Cordoba)
- Ministerio de Ciencia, Tecnologia e Innovacion Productiva (Cordoba)
- Agencia Nacional de Promocion Cientifica y Tecnologica PICT 967
Ask authors/readers for more resources
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 (-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 -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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available