N-linked glycosylation of WNTs

Stable Identifier
R-HSA-3238691
Type
Reaction [omitted]
Species
Homo sapiens
Compartment
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All WNT ligands are predicted to be highly glycosylated. By similarity with WNT ligands in mouse, human WNTs are believed to undergo N-linked glycosylation at multiple asparagine residues and this glycosylation is critical for their secretion (Smolich et al, 1993; Willert et al, 2003, Komekado et al, 2006; Kurayoshi et al, 2007). The mechanism of N-linked glycosylation is not shown here. For a more detailed description, please refer to pathway "Asparagine N-linked glycosylation".

Literature References
PubMed ID Title Journal Year
8167409 Wnt family proteins are secreted and associated with the cell surface

Smolich, BD, McMahon, JA, McMahon, AP, Papkoff, J

Mol. Biol. Cell 1993
22108505 Porcupine-mediated lipidation is required for Wnt recognition by Wls

Herr, P, Basler, K

Dev. Biol. 2012
17117926 Post-translational palmitoylation and glycosylation of Wnt-5a are necessary for its signalling

Kurayoshi, M, Yamamoto, H, Izumi, S, Kikuchi, A

Biochem. J. 2007
12717451 Wnt proteins are lipid-modified and can act as stem cell growth factors

Willert, K, Brown, JD, Danenberg, E, Duncan, AW, Weissman, IL, Reya, T, Yates, JR, Nusse, R

Nature 2003
17397399 Glycosylation and palmitoylation of Wnt-3a are coupled to produce an active form of Wnt-3a

Komekado, H, Yamamoto, H, Chiba, T, Kikuchi, A

Genes Cells 2007
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