Site-specific protein O-glycosylation modulates proprotein processing — Deciphering specific functions of the large polypeptide GalNAc-transferase gene family

• Published in: Biochimica et biophysica acta Vol. 1820; no. 12; pp. 2079 - 2094
• Main Authors: Schjoldager, Katrine T.-B.G., Clausen, Henrik
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.12.2012
• Subjects: Amino Acid Sequence; biosynthesis; Congenital disorder of glycosylation (CDG); Fibroblast Growth Factor-23; GalNAc-transferase (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase); gene expression regulation; gene targeting; genes; Glycoproteins - metabolism; Glycosylation; human cell lines; human diseases; Humans; lipid metabolism; Molecular Sequence Data; Multigene Family; N-Acetylgalactosaminyltransferases - genetics; N-Acetylgalactosaminyltransferases - metabolism; O-glycosylation; phenotype; Polypeptide N-acetylgalactosaminyltransferase; polypeptides; post-translational modification; Pro-protein convertase (PC) processing; Proprotein Convertases - metabolism; Protein Processing, Post-Translational; proteinases; proteins; proteolysis; zinc finger motif; Zinc finger nuclease gene targeting; Congenital disorder of glycosylation (CDG); O-glycosylation; GalNAc-transferase (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase); Zinc finger nuclease gene targeting; Pro-protein convertase (PC) processing

Posttranslational modifications (PTMs) greatly expand the function and regulation of proteins, and glycosylation is the most abundant and diverse PTM. Of the many different types of protein glycosylation, one is quite unique; GalNAc-type (or mucin-type) O-glycosylation, where biosynthesis is initiat...