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The complex world of WNT receptor signalling
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Journal Article
The complex world of WNT receptor signalling
2012
Overview
Key Points
There is bewildering complexity in WNT signal transduction at the cell surface. 19 WNT proteins couple to more than 15 receptors and co-receptors in seven protein families: Frizzled, low-density lipoprotein receptor-related protein 5 (LRP5) and LRP6, receptor Tyr kinase-like orphan receptor 1 (ROR1) and ROR2, protein Tyr kinase 7 (PTK7), receptor Tyr kinase (RYK), muscle skeletal receptor Tyr kinase (MUSK) and the heparan sulphate proteoglycans syndecan and glypican.
Frizzled proteins act as principal WNT receptors and recruit different co-receptors to engage specific subpathways.
WNT receptors and co-receptors are regulated intracellularly by phosphorylation, proteolytic processing and endocytosis.
Endocytosis is a key mechanism, and WNT signalling requires endocytosis, endosomal signalosomes and multivesicular bodies.
Agonists (R-spondins) and antagonists (Dickkopf-related protein 1 (DKK1) and Kremen) regulate receptor and co-receptor internalization to modulate WNT signalling.
The R-spondin family of WNT agonists acts via downstream transmembrane proteins, inlcuding syndecans, Leu-rich repeat-containing G-protein coupled receptor 4 (LGR4) and LGR6 and transmembrane E3 ubiquitin ligases RNF43 and ZNRF3.
Since the discovery of WNTs 30 years ago, it has become clear that this signalling pathway is incredibly complex, using more than 15 receptors and co-receptors. What has emerged is that these proteins form higher-order ligand–receptor complexes that transduce downstream signalling and influence numerous cellular processes.
30 years after the identification of WNTs, their signal transduction has become increasingly complex, with the discovery of more than 15 receptors and co-receptors in seven protein families. The recent discovery of three receptor classes for the R-spondin family of WNT agonists further adds to this complexity. What emerges is an intricate network of receptors that form higher-order ligand–receptor complexes routing downstream signalling. These are regulated both extracellularly by agonists such as R-spondin and intracellularly by post-translational modifications such as phosphorylation, proteolytic processing and endocytosis.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 86
/ Animals
/ Biology
/ Biomedical and Life Sciences
/ Drosophila melanogaster - metabolism
/ Embryos
/ Female
/ Heparan Sulfate Proteoglycans - metabolism
/ Humans
/ Kinases
/ Ligands
/ Male
/ Mice
/ Protein Processing, Post-Translational
/ Proteins
/ Receptor Tyrosine Kinase-like Orphan Receptors - metabolism
