Protein O-mannose β1,2-N-acetylglucosaminyltransferase 1 (POMGNT1) is one of the gene products responsible for α-dystroglycanopathy, which is a type of congenital muscular dystrophy caused by O-mannosyl glycan defects. The originally identified function of POMGNT1 was as a glycosyltransferase that catalyzes the formation of the GlcNAcβ1-2Man linkage of O-mannosyl glycan, but the enzyme function is not essential for α-dystroglycanopathy pathogenesis. Our recent study revealed that the stem domain of POMGNT1 has a carbohydrate-binding ability, which recognizes the GalNAcβ1-3GlcNAc structure. This carbohydrate-binding activity is required for the formation of the ribitol phosphate (RboP)-3GalNAcβ1-3GlcNAc structure by fukutin. This protocol describes methods to assess the carbohydrate-binding activity of the POMGNT1 stem domain.
CITATION STYLE
Manya, H., Kuwabara, N., Kato, R., & Endo, T. (2020). FAM3B/PANDER-Like carbohydrate-binding domain in a glycosyltransferase, POMGNT1. In Methods in Molecular Biology (Vol. 2132, pp. 609–619). Humana Press Inc. https://doi.org/10.1007/978-1-0716-0430-4_52
Mendeley helps you to discover research relevant for your work.