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Dear Colleagues,

The focal adhesion kinase is a key player in providing cellular functions, such as cell adhesion and motility. It has turned out that focal adhesion kinase regulates cell mechanics and hence is crucial for bioengineering, as the microenvironmental cues regulate the expression and activation of focal adhesion kinase. This Special Issue topic encompasses all biological and biophysical research on focal adhesion kinase and interacting molecules in cell culture, tissue culture, or living animal model systems. Additionally, focal adhesion kinase signal transduction processes ranging from the microenvironment to cell–matrix receptors through focal adhesions to the cytoskeleton and the cell nucleus under normal and pathological conditions are included.

Prof. Dr. Claudia Mierke
Guest Editor

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Keywords

focal adhesion kinase
focal adhesion
cell–matrix interaction
cell mechanics and focal adhesion kinase interacting proteins

Published Papers (2 papers)

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Research

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23 pages, 7940 KiB

Open AccessArticle

Quantitative Phase Imaging of Spreading Fibroblasts Identifies the Role of Focal Adhesion Kinase in the Stabilization of the Cell Rear

by Olga Ramaniuk, Zuzana Klímová, Tomáš Groušl and Tomáš Vomastek

Biomolecules 2020, 10(8), 1089; https://doi.org/10.3390/biom10081089 - 22 Jul 2020

Cited by 5 | Viewed by 3504

Abstract

Cells attaching to the extracellular matrix spontaneously acquire front–rear polarity. This self-organization process comprises spatial activation of polarity signaling networks and the establishment of a protruding cell front and a non-protruding cell rear. Cell polarization also involves the reorganization of cell mass, notably the nucleus that is positioned at the cell rear. It remains unclear, however, how these processes are regulated. Here, using coherence-controlled holographic microscopy (CCHM) for non-invasive live-cell quantitative phase imaging (QPI), we examined the role of the focal adhesion kinase (FAK) and its interacting partner Rack1 in dry mass distribution in spreading Rat2 fibroblasts. We found that FAK-depleted cells adopt an elongated, bipolar phenotype with a high central body mass that gradually decreases toward the ends of the elongated processes. Further characterization of spreading cells showed that FAK-depleted cells are incapable of forming a stable rear; rather, they form two distally positioned protruding regions. Continuous protrusions at opposite sides results in an elongated cell shape. In contrast, Rack1-depleted cells are round and large with the cell mass sharply dropping from the nuclear area towards the basal side. We propose that FAK and Rack1 act differently yet coordinately to establish front–rear polarity in spreading cells. Full article

(This article belongs to the Special Issue Focal Adhesion Kinase and Its Role in Cell, Molecular Biology, Cell Mechanics, and Bioengineering)

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Review

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16 pages, 1861 KiB

Open AccessFeature PaperEditor’s ChoiceReview

FAK Structure and Regulation by Membrane Interactions and Force in Focal Adhesions

by Paula Tapial Martínez, Pilar López Navajas and Daniel Lietha

Biomolecules 2020, 10(2), 179; https://doi.org/10.3390/biom10020179 - 24 Jan 2020

Cited by 109 | Viewed by 11258

Abstract

Focal adhesion kinase (FAK) is a non-receptor tyrosine kinase with key roles in the regulation of cell adhesion migration, proliferation and survival. In cancer FAK is a major driver of invasion and metastasis and its upregulation is associated with poor patient prognosis. FAK is autoinhibited in the cytosol, but activated upon localisation into a protein complex, known as focal adhesion complex. This complex forms upon cell adhesion to the extracellular matrix (ECM) at the cytoplasmic side of the plasma membrane at sites of ECM attachment. FAK is anchored to the complex via multiple sites, including direct interactions with specific membrane lipids and connector proteins that attach focal adhesions to the actin cytoskeleton. In migrating cells, the contraction of actomyosin stress fibres attached to the focal adhesion complex apply a force to the complex, which is likely transmitted to the FAK protein, causing stretching of the FAK molecule. In this review we discuss the current knowledge of the FAK structure and how specific structural features are involved in the regulation of FAK signalling. We focus on two major regulatory mechanisms known to contribute to FAK activation, namely interactions with membrane lipids and stretching forces applied to FAK, and discuss how they might induce structural changes that facilitate FAK activation. Full article

(This article belongs to the Special Issue Focal Adhesion Kinase and Its Role in Cell, Molecular Biology, Cell Mechanics, and Bioengineering)

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