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conferenceseries
.com
Volume 10, Issue 8 (Suppl)
J Proteomics Bioinform, an open access journal
ISSN: 0974-276X
Structural Biology 2017
September 18-20, 2017
9
th
International Conference on
Structural Biology
September 18-20, 2017 Zurich, Switzerland
Vesa P Hytonen et al., J Proteomics Bioinform 2017, 10:8(Suppl)
DOI: 10.4172/0974-276X-C1-0100
Mechanical stability of talin rod controls traction force generation and cell migration
Vesa P Hytonen
1
, Rolle Rahikainen
1
, Magdalena von Essen
1
, Markus Schaefer
2
, Lei Qi
3
, Latifeh Azizi
1
, Conor Kelly
1
, Teemu O Ihalainen
1
, Bernhard
Wehrle-Haller
4
, Martin Bastmeyer
2
and
Cai Huang
3
1
University of Tampere, Finland
2
Karlsruhe Institute of Technology, Germany
3
University of Kentucky, USA
4
University of Geneva, Switzerland
T
alin is a central adhesion protein linking β-integrin cytosolic domains to actin fibers. It participates in the transmission of
mechanical signals between extracellular matrix and cell cytoskeleton. Talin rod domain consists of a series of mechanically
vulnerable α-helical subdomains containing binding sites for other adhesion proteins such as vinculin, actin and RIAM.
Force induced unfolding of these rod subdomains has been proposed to act as a cellular mechanosensor, but so far evidence
linking their mechanical stability and cellular response has been lacking. We show that stepwise mechanical destabilization of
talin rod subdomain increases talin and vinculin accumulation into cell-matrix adhesions and decreases cell migration rate.
In addition, mechanical destabilization of talin subdomain was found to decrease cellular traction force generation and to
promote the formation of adhesions on fibronectin over vitronectin. Experiments with truncated talin forms confirmed the
mechanosensory role of the talin subdomain and excluded the possibility that the observed effects are caused solely by the
release of talin autoinhibition. We demonstrate that by modulating the mechanical stability of an individual talin rod sub-
domain, it is possible to affect traction force generation, ECM sensing and consequently highly coordinated processes such as
cell migration. Our results suggest that talin acts as a mechanosensor and is responsible for controlling the cellular processes
dependent on mechanical signals and cellular mechanosensing.
Biography
Vesa P Hytonen is a Head of the Protein Dynamics research group in BioMediTech at the University of Tampere, Finland. After graduating as a PhD scholar from the
University of Jyväskylä, Finland in 2005, he has conducted Post-doctoral training at ETH Zurich, Switzerland from 2005-2007. He then continued as a Post-Doctoral
researcher at the University of Tampere and established independent research group in 2010. He is currently working as Associate Professor at the University of
Tampere. His research interests are Mechanobiology, Protein Engineering and Vaccine research and authored more than 100 scientific articles.
vesa.hytonen@uta.fi