Talin-mediated force transmission and talin rod domain unfolding independently regulate adhesion signaling

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http://hdl.handle.net/10138/311486

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Rahikainen , R , Öhman , T , Turkki , P , Varjosalo , M & Hytönen , V P 2019 , ' Talin-mediated force transmission and talin rod domain unfolding independently regulate adhesion signaling ' , Journal of Cell Science , vol. 132 , no. 7 , 226514 . https://doi.org/10.1242/jcs.226514

Title: Talin-mediated force transmission and talin rod domain unfolding independently regulate adhesion signaling
Author: Rahikainen, Rolle; Öhman, Tiina; Turkki, Paula; Varjosalo, Markku; Hytönen, Vesa P.
Contributor: University of Helsinki, Institute of Biotechnology
University of Helsinki, Molecular Systems Biology
Date: 2019-04
Language: eng
Number of pages: 14
Belongs to series: Journal of Cell Science
ISSN: 0021-9533
URI: http://hdl.handle.net/10138/311486
Abstract: Talin protein is one of the key components in integrin-mediated adhesion complexes. Talins transmit mechanical forces between beta-integrin and actin, and regulate adhesion complex composition and signaling through the force-regulated unfolding of talin rod domain. Using modified talin proteins, we demonstrate that these functions contribute to different cellular processes and can be dissected. The transmission of mechanical forces regulates adhesion complex composition and phosphotyrosine signaling even in the absence of the mechanically regulated talin rod subdomains. However, the presence of the rod subdomains and their mechanical activation are required for the reinforcement of the adhesion complex, cell polarization and migration. Talin rod domain unfolding was also found to be essential for the generation of cellular signaling anisotropy, since both insufficient and excess activity of the rod domain severely inhibited cell polarization. Utilizing proteomics tools, we identified adhesome components that are recruited and activated either in a talin rod-dependent manner or independently of the rod subdomains. This study clarifies the division of roles between the force-regulated unfolding of a talin protein (talin 1) and its function as a physical linker between integrins and the cytoskeleton.
Subject: BioID
Focal adhesion
Mechanobiology
Phosphoproteomics
Protein engineering
Talin
CELL POLARIZATION
FOCAL ADHESIONS
RHOA ACTIVITY
VINCULIN
INTEGRIN
PROTEIN
RECRUITMENT
ACTIVATION
TENSION
BINDING
1182 Biochemistry, cell and molecular biology
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