Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

Wnt morphogens are secreted signalling proteins that play leading roles in embryogenesis and tissue homeostasis throughout life. Wnt signalling is controlled by multiple mechanisms, including posttranslational modification of Wnts, antagonist binding (to Wnts or their receptors), and regulation of the availability of Wnt receptors. Recent crystallographic, structure-guided biophysical and cell-based studies have advanced our understanding of how Wnt signalling is regulated at the cell surface. Structures include Wnt in complex with the cysteine-rich domain (CRD) of Frizzled, extracellular fragments of Wnt co-receptor LRP6, LRP6-binding antagonists Dickkopf and Sclerostin, antagonists 5T4/WAIF1 and Wnt inhibitory factor 1 (WIF-1), as well as Frizzled-ubiquitin ligases ZNRF3/RNF43 (in isolation and in complexes with Wnt signalling promoters R-spondins and LGR5). We review recent discoveries and remaining questions.

Original publication

DOI

10.1016/j.sbi.2014.10.003

Type

Journal article

Journal

Curr Opin Struct Biol

Publication Date

12/2014

Volume

29

Pages

77 - 84

Keywords

Animals, Binding Sites, Cysteine, DNA-Binding Proteins, Extracellular Matrix Proteins, Frizzled Receptors, Humans, Low Density Lipoprotein Receptor-Related Protein-5, Low Density Lipoprotein Receptor-Related Protein-6, Protein Binding, Protein Conformation, Ubiquitin-Protein Ligases, Wnt Proteins, Wnt Signaling Pathway