Abl and Canoe/Afadin mediate mechanotransduction at tricellular junctions.
basic_science · Level V
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- Record sourced from PubMed, PMID 33243859.
- Also identified by DOI 10.1126/science.aba5528 and PMC identifier 8559527.
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Abstract
Epithelial structure is generated by the dynamic reorganization of cells in response to mechanical forces. Adherens junctions transmit forces between cells, but how cells sense and respond to these forces in vivo is not well understood. We identify a mechanotransduction pathway involving the Abl tyrosine kinase and Canoe/Afadin that stabilizes cell adhesion under tension at tricellular junctions in the <i>Drosophila</i> embryo. Canoe is recruited to tricellular junctions in response to actomyosin contractility, and this mechanosensitivity requires Abl-dependent phosphorylation of a conserved tyrosine in the Canoe actin-binding domain. Preventing Canoe tyrosine phosphorylation destabilizes tricellular adhesion, and anchoring Canoe at tricellular junctions independently of mechanical inputs aberrantly stabilizes adhesion, arresting cell rearrangement. These results identify a force-responsive mechanism that stabilizes tricellular adhesion under tension during epithelial remodeling.
Medical subject headings
- Cell Adhesion
- Drosophila Proteins
- Intercellular Junctions
- Mechanotransduction, Cellular
- Protein-Tyrosine Kinases