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FAK-Dependent Cell Motility and Cell Elongation

Laboratory of Human Anatomy and Cell Biology, Faculty of Health Sciences, Tsukuba University of Technology Tsukuba-city, Ibaraki 305-8520, Japan
Cells 2020, 9(1), 192; https://doi.org/10.3390/cells9010192 (registering DOI)
Received: 10 December 2019 / Revised: 2 January 2020 / Accepted: 8 January 2020 / Published: 12 January 2020
(This article belongs to the Section Cell Motility and Adhesion)
Fibroblastic cells show specific substrate selectivity for typical cell–substrate adhesion. However, focal adhesion kinase (FAK) contributes to controlling the regulation of orientation and polarity. When fibroblasts attach to micropatterns, tyrosine-phosphorylated proteins and FAK are both detected along the inner border between the adhesive micropatterns and the nonadhesive glass surface. FAK likely plays important roles in regulation of cell adhesion to the substrate, as FAK is a tyrosine-phosphorylated protein that acts as a signal transduction molecule at sites of cell–substrate attachment, called focal adhesions. FAK has been suggested to play a role in the attachment of cells at adhesive micropatterns by affecting cell polarity. Therefore, the localization of FAK might play a key role in recognition of the border of the cell with the adhesive micropattern, thus regulating cell polarity and the cell axis. This review discusses the regulation and molecular mechanism of cell proliferation and cell elongation by FAK and its associated signal transduction proteins. View Full-Text
Keywords: FAK; focal adhesion; c-Src; cell motility; cell elongation FAK; focal adhesion; c-Src; cell motility; cell elongation
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Katoh, K. FAK-Dependent Cell Motility and Cell Elongation. Cells 2020, 9, 192.

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