Wnt proteins are conserved signalling molecules that have an essential role in regulating diverse processes during embryogenesis and adult tissue homoeostasis. Wnts are post-translationally modified by palmitoylation, which is essential for Wnt secretion and function. Intriguingly, the crystal structure of XWnt8 in complex with the extracellular domain of the Frizzled 8 cysteine-rich domain (Fzd8-CRD) revealed that Wnts use the fatty acid as a ‘hotspot’ residue to engage its receptor, which is a unique mode of receptor-ligand recognition. In addition, there are several lines of evidence suggesting that Wnts engage several signalling modulators and alternative receptors by means of fatty acids as a critical contact residue. In the present article, we review our current understanding of Wnt acylation and its functional role in Wnt signalling regulation.
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April 2015
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Conference Article|
April 07 2015
Wnt acylation and its functional implication in Wnt signalling regulation
Claudia Y. Janda;
Claudia Y. Janda
*Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, CA 94305, U.S.A.
†Department of Molecular and Cellular Physiology, and Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, U.S.A.
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K. Christopher Garcia
K. Christopher Garcia
1
*Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, CA 94305, U.S.A.
†Department of Molecular and Cellular Physiology, and Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, U.S.A.
1To whom correspondence should be addressed (emailkcgarcia@stanford.edu).
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Publisher: Portland Press Ltd
Received:
September 17 2014
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2015 Biochemical Society
2015
Biochem Soc Trans (2015) 43 (2): 211–216.
Article history
Received:
September 17 2014
Citation
Claudia Y. Janda, K. Christopher Garcia; Wnt acylation and its functional implication in Wnt signalling regulation. Biochem Soc Trans 1 April 2015; 43 (2): 211–216. doi: https://doi.org/10.1042/BST20140249
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