Abstract
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.
Highlights
When cultured on a glass surface, the plasma membrane of fibroblastic cells begins to move from the distal end to the leading edge [1]
The cell membranes are composed of the plasma membrane, which is mechanically stabilized by a thick macromolecular network that is composed of the actin filaments
The functions of focal adhesion kinase (FAK) at the time of stress fiber and focal adhesion formation were examined, and the results indicated that the activation of ROCK induced the formation of stress fibers and focal adhesions in FAK knockout (FAK-null or FAK−/− ) cells [35]
Summary
When cultured on a glass surface, the plasma membrane of fibroblastic cells begins to move from the distal end to the leading edge [1]. FAK activation involves integrin receptor accumulation and binding to the ECM proteins, which results in the dimerization of FAK [24] This FAK dimerization induces autophosphorylation of FAK at pY397, resulting in the Src-mediated phosphorylation of the FAK kinase domain (pY576 or pY577), leading to the formation of the active FAK–Src complex [23,25]. Some signal transduction proteins, such as FAK, c-Src, Rho A, and integrin, are localized along with these proteins in close association with focal adhesions These observations strongly suggest that the focal adhesions play roles in the connection between the plasma membrane of the cell and substrate, and in transferring specific signals from the outside to the inside of the cell. This protein complex enhances the membrane affinity of Rac and further activates the above-mentioned kinase pathway
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