FAM3B/PANDER-Like Carbohydrate-Binding Domain in a Glycosyltransferase, POMGNT1.
Carbohydrate-binding
FAM3B
Fukutin
Glycosyltransferase
O-Mannosyl glycan
PANDER
POMGNT1
α-Dystroglycan
α-Dystroglycanopathy
Journal
Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969
Informations de publication
Date de publication:
2020
2020
Historique:
entrez:
20
4
2020
pubmed:
20
4
2020
medline:
9
3
2021
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 32306360
doi: 10.1007/978-1-0716-0430-4_52
doi:
Substances chimiques
Carbohydrates
0
Cytokines
0
FAM3B protein, human
0
Neoplasm Proteins
0
N-Acetylglucosaminyltransferases
EC 2.4.1.-
protein O-mannose beta-1,2-N-acetylglucosaminyltransferase
EC 2.4.1.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM