Please use this identifier to cite or link to this item: https://doi.org/10.1038/ncb2370
Title: Fibroblast polarization is a matrix-rigidity-dependent process controlled by focal adhesion mechanosensing
Authors: Prager-Khoutorsky, M.
Lichtenstein, A.
Krishnan, R.
Rajendran, K.
Mayo, A.
Kam, Z.
Geiger, B.
Bershadsky, A.D. 
Issue Date: Dec-2011
Citation: Prager-Khoutorsky, M., Lichtenstein, A., Krishnan, R., Rajendran, K., Mayo, A., Kam, Z., Geiger, B., Bershadsky, A.D. (2011-12). Fibroblast polarization is a matrix-rigidity-dependent process controlled by focal adhesion mechanosensing. Nature Cell Biology 13 (12) : 1457-1465. ScholarBank@NUS Repository. https://doi.org/10.1038/ncb2370
Abstract: Cell elongation and polarization are basic morphogenetic responses to extracellular matrix adhesion. We demonstrate here that human cultured fibroblasts readily polarize when plated on rigid, but not on compliant, substrates. On rigid surfaces, large and uniformly oriented focal adhesions are formed, whereas cells plated on compliant substrates form numerous small and radially oriented adhesions. Live-cell monitoring showed that focal adhesion alignment precedes the overall elongation of the cell, indicating that focal adhesion orientation may direct cell polarization. siRNA-mediated knockdown of 85 human protein tyrosine kinases (PTKs) induced distinct alterations in the cell polarization response, as well as diverse changes in cell traction force generation and focal adhesion formation. Remarkably, changes in rigidity-dependent traction force development, or focal adhesion mechanosensing, were consistently accompanied by abnormalities in the cell polarization response. We propose that the different stages of cell polarization are regulated by multiple, PTK-dependent molecular checkpoints that jointly control cell contractility and focal-adhesion-mediated mechanosensing. © 2011 Macmillan Publishers Limited. All rights reserved.
Source Title: Nature Cell Biology
URI: http://scholarbank.nus.edu.sg/handle/10635/126614
ISSN: 14657392
DOI: 10.1038/ncb2370
Appears in Collections:Staff Publications

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