Reactome | N-linked glycosylation of WNTs

N-linked glycosylation of WNTs

Stable Identifier

R-HSA-3238691

Type

Reaction [omitted]

Species

Homo sapiens

Compartment

endoplasmic reticulum lumen

ReviewStatus

5/5

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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
22108505	Porcupine-mediated lipidation is required for Wnt recognition by Wls Herr, P, Basler, K	Dev. Biol.	2012
8167409	Wnt family proteins are secreted and associated with the cell surface Smolich, BD, McMahon, JA, McMahon, AP, Papkoff, J	Mol. Biol. Cell	1993
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