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αV-Integrins Are Required for Mechanotransduction in MDCK Epithelial Cells
Author(s) -
Terhi P. Teräväinen,
Satu-Marja Myllymäki,
Jens Friedrichs,
Nico Strohmeyer,
José V. Moyano,
Chuanyue Wu,
Karl S. Matlin,
Daniel J. Müller,
Aki Manninen
Publication year - 2013
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0071485
Subject(s) - focal adhesion , integrin , microbiology and biotechnology , mechanotransduction , vinculin , extracellular matrix , ptk2 , cell adhesion , actin cytoskeleton , paxillin , collagen receptor , biology , cytoskeleton , chemistry , cell , signal transduction , protein kinase c , biochemistry , mitogen activated protein kinase kinase
The properties of epithelial cells within tissues are regulated by their immediate microenvironment, which consists of neighboring cells and the extracellular matrix (ECM). Integrin heterodimers orchestrate dynamic assembly and disassembly of cell-ECM connections and thereby convey biochemical and mechanical information from the ECM into cells. However, the specific contributions and functional hierarchy between different integrin heterodimers in the regulation of focal adhesion dynamics in epithelial cells are incompletely understood. Here, we have studied the functions of RGD-binding αV-integrins in a Madin Darby Canine Kidney (MDCK) cell model and found that αV-integrins regulate the maturation of focal adhesions (FAs) and cell spreading. αV-integrin-deficient MDCK cells bound collagen I (Col I) substrate via α2β1-integrins but failed to efficiently recruit FA components such as talin, focal adhesion kinase (FAK), vinculin and integrin-linked kinase (ILK). The apparent inability to mature α2β1-integrin-mediated FAs and link them to cellular actin cytoskeleton led to disrupted mechanotransduction in αV-integrin deficient cells seeded onto Col I substrate.

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