Epithelial Monolayers Coalesce on a Viscoelastic Substrate through Redistribution of Vinculin
| Autor: | Siew Ping Han, Jun Zhong, Ai Kia Yip, Ji Yun Zheng, Nicolas Boichat, Paul Matsudaira, Yi-Jen Chiu, Shi Wen Zhu |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Biophysics Acrylic Resins Viscoelastic Substances Cell junction Models Biological Viscoelasticity Madin Darby Canine Kidney Cells Focal adhesion 03 medical and health sciences Mice Dogs Cell Movement Monolayer Animals Focal Adhesions Microscopy Confocal biology Chemistry Cadherin Substrate (chemistry) Epithelial Cells Vinculin Cell biology Culture Media 030104 developmental biology Cell Biophysics biology.protein |
| Zdroj: | Biophysical Journal |
| ISSN: | 1542-0086 |
| Popis: | The mechanical properties of the microenvironment play a large role in influencing cellular behavior. In particular, the tradeoff between substrate viscosity and elasticity on collective cell migration by adherent cells is highly physiologically relevant, but remains poorly understood. To investigate the specific effects of viscous substrates, we plated epithelial monolayers onto polydimethylsiloxane substrata with a range of viscosities and elasticities. We found that on viscoelastic substrates the monolayers underwent rapid and coordinated movement to generate cell-free areas. To understand the molecular mechanism of this coordinated movement, we imaged various structural and signaling proteins at cell-cell and cell-matrix junctions. Through quantitative image analysis of monolayer disruption and subcellular protein redistribution, we show that the mechanosensor protein, vinculin, is necessary and sufficient for this viscous response, during which it is lost from focal adhesions and recruited by the cadherin complex to intercellular junctions. In addition, the viscous response is dependent upon and enhanced by actomyosin contractility. Our results implicate vinculin translocation in a molecular switching mechanism that senses substrate viscoelasticity and associates with actomyosin contractility. |
| Databáze: | OpenAIRE |
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