Control of mucin-type O-glycosylation: a classification of the polypeptide GalNAc-transferase gene family.

By E. Bennett, U. Mandel, H. Clausen, T. Gerken, T. A. Fritz, L. Tabak. Glycobiology, 2012

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New developments in goblet cell mucus secretion and function (2015, neutral): “The first appearance of molecules with protein domains typical to polymeric mucins was among metazoans as was the appearance of glycosyltransferases necessary for decorating the mucin protein core.(2,3) Together, this allowed the biosynthesis of molecules that are virtually indigestible by the host’”
Mucin glycan foraging in the human gut microbiome (2015, background): “The synthesis of mucin oligosaccharides starts with the transfer of N-acetylgalactosamine (GalNAc) to Ser and Thr residues of the mucin core (Bennett et al., 2012).”
Biological roles of glycans (2016, background): “Further complexity has arisen from the realization that there are multiple isozymes of some glycosyltransferases (417, 418), and that posttranscriptional regulation by microRNAs is occurring (419, 420).”
The mucus and mucins of the goblet cells and enterocytes provide the first defense line of the gastrointestinal tract and interact with the immune system (2014, neutral): “After the ER, the dimers pass into the Golgi apparatus, where O-glycosylation takes place by adding GalNAc to the serine and threonine residues of the two central PTS domains (75).”