Abl and Canoe/Afadin mediate mechanotransduction at tricellular junctions
Author(s) -
Huapeng H. Yu,
Jennifer A. Zallen
Publication year - 2020
Publication title -
science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 12.556
H-Index - 1186
eISSN - 1095-9203
pISSN - 0036-8075
DOI - 10.1126/science.aba5528
Subject(s) - mechanotransduction , microbiology and biotechnology , phosphorylation , regulator , biology , adherens junction , adhesion , tight junction , abl , chemistry , cadherin , signal transduction , tyrosine kinase , genetics , gene , cell , organic chemistry
Tension where multiple cells meet Cells exist in varying environments and must respond to specific stimuli. During development, epithelial cells need to rapidly reorganize under tension without compromising epithelial integrity. Yuet al. demonstrate thatDrosophila epithelial cells achieve this by transiently stabilizing adhesion at tricellular junctions where three cells meet (see the Perspective by Raghavan and Vasioukhin). The conserved adhesion regulator Canoe/Afadin is recruited to tricellular junctions under tension within seconds and dissociates when tension is released through a mechanism that requires Abl-dependent tyrosine phosphorylation. These results identify an in vivo mechanotransduction pathway that dynamically couples tricellular adhesion with physiological forces, allowing cells to rapidly modulate their behavior in response to mechanical changes in their environment.Science , this issue p.eaba5528 ; see also p.1036
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