期刊
JOURNAL OF CELL SCIENCE
卷 129, 期 9, 页码 1843-1854出版社
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.185447
关键词
E-cadherin; Integrin; Mechanotransduction; Traction force microscopy; Magnetic twisting cytometry; Cell signaling
类别
资金
- National Science Foundation [CMMI 1029871, 1462739]
- National Institutes of Health [R01 GM097443]
- Shen Postdoctoral Fellowship
- Directorate For Engineering
- Div Of Civil, Mechanical, & Manufact Inn [1462739] Funding Source: National Science Foundation
This report elucidates an E-cadherin-based force-transduction pathway that triggers changes in cell mechanics through a mechanism requiring epidermal growth factor receptor (EGFR), phosphoinositide 3-kinase (PI3K), and the downstream formation of new integrin adhesions. This mechanism operates in addition to local cytoskeletal remodeling triggered by conformational changes in the E-cadherin-associated protein alpha-catenin, at sites of mechanical perturbation. Studies using magnetic twisting cytometry (MTC), together with traction force microscopy (TFM) and confocal imaging identified force-activated E-cadherin-specific signals that integrate cadherin force transduction, integrin activation and cell contractility. EGFR is required for the downstream activation of PI3K and myosin-II-dependent cell stiffening. Our findings also demonstrated that alpha-catenin-dependent cytoskeletal remodeling at perturbed E-cadherin adhesions does not require cell stiffening. These results broaden the repertoire of E-cadherin-based force transduction mechanisms, and define the force-sensitive signaling network underlying the mechano-chemical integration of spatially segregated adhesion receptors.
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