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Identification of EPS8 as a Dvl1-associated molecule
M Inobe1, K i Katsube, Y Miyagoe
1Department of Molecular Genetics, National Institute of Neuroscience, Kodaira, Tokyo, 187-8502, Japan.
Biochemical and Biophysical Research Communications
|December 3, 1999
Summary
Dishevelled (Dsh) interacts with EPS8, a protein regulated by EGF receptor (EGFR) signaling. This interaction influences phosphorylation events and suggests a role for Dsh in developmental signaling pathways.
Area of Science:
- Molecular Biology
- Developmental Biology
- Cell Signaling
Background:
- Dishevelled (Dsh) is a key mediator in Wingless (Wg) and Frizzled (Fz) signaling pathways.
- Understanding Dsh interactions is crucial for deciphering its role in cellular processes.
Purpose of the Study:
- To identify novel Dsh-interacting proteins using yeast two-hybrid screening.
- To investigate the functional consequences of the interaction between Dsh and EPS8.
Main Methods:
- Yeast two-hybrid screening to identify interacting partners of Dvl1 (a Dsh homolog).
- In vitro interaction assays and transfection studies to confirm and analyze the Dvl1-EPS8 interaction.
- Immunohistochemistry to examine expression patterns during organogenesis.
Main Results:
- EPS8, an EGF receptor (EGFR) substrate, was identified as a Dvl1-interacting protein.
- Dvl1 and EPS8 exhibit mutual regulation: Dvl1 is hyperphosphorylated by EPS8, and Dvl1 inhibits EGFR-mediated tyrosine phosphorylation of EPS8.
- Dvl1 and EPS8 expression show overlapping patterns in specific tissues during organogenesis.
Conclusions:
- The interaction between Dvl1 and EPS8 suggests a crosstalk between Dsh-mediated pathways and receptor tyrosine kinase signaling.
- This interaction likely plays a significant role in developmental events and organogenesis.