title: Integrin-linked kinase regulates cellular mechanics facilitating the motility in 3D extracellular matrices.
abstract: The motility of cells plays an important role for many processes such as wound healing and malignant progression of cancer. The efficiency of cell motility is affected by the microenvironment. The connection between the cell and its microenvironment is facilitated by cell-matrix adhesion receptors and upon their activation focal adhesion proteins such as integrin-linked kinase (ILK) are recruited to sites of focal adhesion formation. In particular, ILK connects cell-matrix receptors to the actomyosin cytoskeleton. However, ILK's role in cell mechanics regulating cellular motility in 3D collagen matrices is still not well understood. We suggest that ILK facilitates 3D motility by regulating cellular mechanical properties such as stiffness and force transmission. Thus, ILK wild-type and knock-out cells are analyzed for their ability to migrate on 2D substrates serving as control and in dense 3D extracellular matrices. Indeed, ILK wild-type cells migrated faster on 2D substrates and migrated more numerous and deeper in 3D matrices. Hence, we analyzed cellular deformability, Young's modulus (stiffness) and adhesion forces. We found that ILK wild-type cells are less deformable (stiffer) and produce higher cell-matrix adhesion forces compared to ILK knock-out cells. Finally, ILK is essential for providing cellular mechanical stiffness regulating 3D motility.
authors.affiliation: University of Leipzig, Faculty of Physics and Earth Science, Institute for Experimental Physics I, Biological Physics Division, Linnestrasse 5, 04103 Leipzig, Germany.
authors.forename: Tom
authors.initials: T
authors.lastname: Kunschmann
authors.affiliation: University of Leipzig, Faculty of Physics and Earth Science, Institute for Experimental Physics I, Biological Physics Division, Linnestrasse 5, 04103 Leipzig, Germany.
authors.forename: Stefanie
authors.initials: S
authors.lastname: Puder
authors.affiliation: University of Leipzig, Faculty of Physics and Earth Science, Institute for Experimental Physics I, Biological Physics Division, Linnestrasse 5, 04103 Leipzig, Germany.
authors.forename: Tony
authors.initials: T
authors.lastname: Fischer
authors.affiliation: University of Leipzig, Faculty of Physics and Earth Science, Institute for Experimental Physics I, Biological Physics Division, Linnestrasse 5, 04103 Leipzig, Germany.
authors.forename: Jeremy
authors.initials: J
authors.lastname: Perez
authors.affiliation: University of Leipzig, Faculty of Physics and Earth Science, Institute for Experimental Physics I, Biological Physics Division, Linnestrasse 5, 04103 Leipzig, Germany.
authors.forename: Nils
authors.initials: N
authors.lastname: Wilharm
authors.affiliation: University of Leipzig, Faculty of Physics and Earth Science, Institute for Experimental Physics I, Biological Physics Division, Linnestrasse 5, 04103 Leipzig, Germany. Electronic address: claudia.mierke@uni-leipzig.de.
authors.forename: Claudia Tanja
authors.initials: CT
authors.lastname: Mierke
mesh_terms: D008841:Actin Cytoskeleton / Q000378:metabolism* / Q000648:ultrastructure; D000818:Animals; D001696:Biomechanical Phenomena; D002448:Cell Adhesion; D018929:Cell Culture Techniques; D002465:Cell Movement; D055119:Elastic Modulus; D005109:Extracellular Matrix / Q000378:metabolism* / Q000648:ultrastructure; D005347:Fibroblasts / Q000378:metabolism* / Q000648:ultrastructure; D022001:Focal Adhesions / Q000378:metabolism* / Q000648:ultrastructure; D015870:Gene Expression; D051379:Mice; D017346:Protein Serine-Threonine Kinases / Q000172:deficiency / Q000235:genetics*; D015398:Signal Transduction; D013314:Stress, Mechanical; D000099200:Scaffold Protein ILK
chemical_list: D017346:Protein Serine-Threonine Kinases; D000099200:Scaffold Protein ILK