PUBLICATION

An integrated model for Gpr124 function in Wnt7a/b signaling among vertebrates

Authors
America, M., Bostaille, N., Eubelen, M., Martin, M., Stainier, D.Y.R., Vanhollebeke, B.
ID
ZDB-PUB-220602-17
Date
2022
Source
Cell Reports   39: 110902 (Journal)
Registered Authors
Stainier, Didier, Vanhollebeke, Benoit
Keywords
BBB, CP: Cell biology, Dlg4, Gpr124, Magi3, Reck, Wnt/β-catenin signaling, Wnt7a, Wnt7b, blood-brain barrier, brain angiogenesis
MeSH Terms
  • Animals
  • Central Nervous System
  • Humans
  • Ligands
  • Mice
  • Receptors, G-Protein-Coupled*/metabolism
  • Wnt Signaling Pathway*
  • Zebrafish
PubMed
35649360 Full text @ Cell Rep.
Abstract
Within the central nervous system, Wnt7a/b are unambiguously discriminated from other Wnt ligands by an endothelial receptor complex made of the glycosylphosphatidylinositol (GPI)-anchored Reck and the adhesion G protein-coupled receptor (GPCR) Gpr124. Reck is a Wnt7a/b-specific receptor, while Gpr124 facilitates the delivery of Reck-bound Wnt7a/b ligands to Frizzled, through partially characterized mechanisms. We report that, in zebrafish, the Gpr124-Frizzled interactions are dominated by intracellular scaffolds that exploit the striking molecular mimicry between Gpr124 and Frizzled intracellular domains (ICDs): an internal Dvl-binding motif and a C-terminal ETTV motif that recruits Dlg4 and Magi3. By contrast, mammalian Gpr124 receptors exhibit an ICD-independent interaction mechanism governed by species-specific attributes of their transmembrane and extracellular domains. This mechanism seemingly evolved to replace the Dvl-mediated mechanism. By contrasting zebrafish, mouse, and human Gpr124, this study provides insights into the evolution of Gpr124/Reck function across the vertebrate clade, a receptor complex uniquely implicated in Wnt ligand-specific cellular responses.
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Human Disease / Model
Sequence Targeting Reagents
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Mapping