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E-cadherin engagement stimulates tyrosine phosphorylation
1Department of Cell Biology and Anatomy, University of North Carolina at Chapel Hill 27599-7090, USA.
Cell Adhesion and Communication
|March 1, 1997
Summary
E-cadherin engagement rapidly increases tyrosine phosphorylation at cell-cell junctions, involving proteins like ras-GAP. This phosphorylation is not essential for forming adherens junctions.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Cadherins are crucial cell adhesion molecules forming adherens junctions with catenins.
- Signaling pathways initiated by cadherin engagement are not well understood.
Purpose of the Study:
- To investigate signaling pathways triggered by E-cadherin-mediated cell-cell adhesion.
- To identify proteins involved in cadherin-induced signaling.
Main Methods:
- Studied tyrosine phosphorylation changes upon E-cadherin engagement in cells.
- Used antibody aggregation of E-cadherin to mimic cell adhesion.
- Identified phosphorylated proteins using biochemical methods.
Main Results:
- E-cadherin engagement rapidly increased tyrosine phosphorylation at cell-cell contacts.
- This phosphorylation could be induced by E-cadherin aggregation with antibodies.
- Phosphorylated proteins included ras-GAP and differed from integrin-adhesion substrates.
- E-cadherin-mediated tyrosine phosphorylation was not required for adherens junction assembly.
Conclusions:
- E-cadherin engagement activates rapid tyrosine phosphorylation signaling at cell-cell junctions.
- This pathway involves specific proteins like ras-GAP.
- Adherens junction formation is independent of this cadherin-triggered phosphorylation event.