ZFIN ID: ZDB-PUB-130710-128
Gpr125 modulates Dishevelled distribution and planar cell polarity signaling
Li, X., Roszko, I., Sepich, D.S., Ni, M., Hamm, H.E., Marlow, F.L., and Solnica-Krezel, L.
Date: 2013
Source: Development (Cambridge, England)   140(14): 3028-3039 (Journal)
Registered Authors: Li, Xin, Marlow, Florence, Roszko, Isabelle, Sepich, Diane, Solnica-Krezel, Lilianna
Keywords: gastrulation movements, convergence and extension, facial branchiomotor neuron, zebrafish
MeSH Terms:
  • Adaptor Proteins, Signal Transducing/metabolism
  • Animals
  • Cell Movement*
  • Cell Polarity*
  • Embryo, Nonmammalian/cytology
  • Embryo, Nonmammalian/metabolism
  • Mutation
  • Phosphoproteins/metabolism
  • Receptors, G-Protein-Coupled/genetics
  • Receptors, G-Protein-Coupled/metabolism*
  • Wings, Animal/cytology
  • Wings, Animal/embryology
  • Wnt Signaling Pathway*
  • Zebrafish/embryology*
  • Zebrafish/metabolism*
  • Zebrafish Proteins/genetics
  • Zebrafish Proteins/metabolism*
PubMed: 23821037 Full text @ Development

During vertebrate gastrulation, Wnt/planar cell polarity (PCP) signaling orchestrates polarized cell behaviors underlying convergence and extension (C&E) movements to narrow embryonic tissues mediolaterally and lengthen them anteroposteriorly. Here, we have identified Gpr125, an adhesion G protein-coupled receptor, as a novel modulator of the Wnt/PCP signaling system. Excess Gpr125 impaired C&E movements and the underlying cell and molecular polarities. Reduced Gpr125 function exacerbated the C&E and facial branchiomotor neuron (FBMN) migration defects of embryos with reduced Wnt/PCP signaling. At the molecular level, Gpr125 recruited Dishevelled to the cell membrane, a prerequisite for Wnt/PCP activation. Moreover, Gpr125 and Dvl mutually clustered one another to form discrete membrane subdomains, and the Gpr125 intracellular domain directly interacted with Dvl in pull-down assays. Intriguingly, Dvl and Gpr125 were able to recruit a subset of PCP components into membrane subdomains, suggesting that Gpr125 may modulate the composition of Wnt/PCP membrane complexes. Our study reveals a role for Gpr125 in PCP-mediated processes and provides mechanistic insight into Wnt/PCP signaling.