Gpr125 modulates Dishevelled distribution and planar cell polarity signaling
- Authors
- Li, X., Roszko, I., Sepich, D.S., Ni, M., Hamm, H.E., Marlow, F.L., and Solnica-Krezel, L.
- ID
- ZDB-PUB-130710-128
- 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.