B3GnT2
LRP6
Wnt signalling
Wnt/β-catenin
glycosylation
polylactosamine
Journal
Cells
ISSN: 2073-4409
Titre abrégé: Cells
Pays: Switzerland
ID NLM: 101600052
Informations de publication
Date de publication:
10 03 2023
10 03 2023
Historique:
received:
31
01
2023
revised:
07
03
2023
accepted:
08
03
2023
medline:
30
3
2023
entrez:
29
3
2023
pubmed:
30
3
2023
Statut:
epublish
Résumé
Reception of Wnt signals by cells is predominantly mediated by Frizzled receptors in conjunction with a co-receptor, the latter being LRP6 or LRP5 for the Wnt/β-catenin signalling pathway. It is important that cells maintain precise control of receptor activation events in order to properly regulate Wnt/β-catenin signalling as aberrant signalling can result in disease in humans. Phosphorylation of the intracellular domain (ICD) of LRP6 is well known to regulate Wntβ-catenin signalling; however, less is known for regulatory post-translational modification events within the extracellular domain (ECD). Using a cell culture-based expression screen for functional regulators of LRP6, we identified a glycosyltransferase, B3GnT2-like, from a teleost fish (medaka) cDNA library, that modifies LRP6 and regulates Wnt/β-catenin signalling. We provide both gain-of-function and loss-of-function evidence that the single human homolog, B3GnT2, promotes extension of polylactosamine chains at multiple
Identifiants
pubmed: 36980204
pii: cells12060863
doi: 10.3390/cells12060863
pmc: PMC10047360
pii:
doi:
Substances chimiques
beta Catenin
0
Low Density Lipoprotein Receptor-Related Protein-6
0
Glycosyltransferases
EC 2.4.-
LRP6 protein, human
0
B3GNT2 protein, human
EC 2.4.1.149
N-Acetylglucosaminyltransferases
EC 2.4.1.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
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