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Vesa P Hytönen

Vesa P Hytönen

University of Tampere, Finland

Title: Mechanical Stability of Talin Rod Controls Traction Force Generation and Cell Migration

Biography

Biography: Vesa P Hytönen

Abstract

Talin 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.

References:

  1. von Essen M, Rahikainen R, Oksala N, Raitoharju E, Seppälä I, Mennander A, Sioris T, Kholová I, Klopp N, Illig T, Karhunen PJ, Kähönen M, Lehtimäki T, Hytönen VP (2016) Talin and vinculin are downregulated in atherosclerotic plaque; Tampere Vascular Study. Atherosclerosis. 255:43-53.
  2. Qi L, Jafari N, Li X, Chen Z, Li L, Hytönen VP, Goult BT, Zhan CG, Huang C (2016) Talin2-mediated traction force drives matrix degradation and cell invasion. J Cell Sci. 129:3661-3674.
  3. Haining AW, von Essen M, Attwood SJ, Hytönen VP, Del Río Hernández A (2016) All Subdomains of the Talin Rod Are Mechanically Vulnerable and May Contribute To Cellular Mechanosensing. ACS Nano 10:6648-58.
  4. Hytönen VP, Wehrle-Haller B (2016) Mechanosensing in cell-matrix adhesions - Converting tension into chemical signals. Exp Cell Res. 343:35-41.
  5. Hytönen VP, Vogel V (2008) How force might activate talin's vinculin binding sites: SMD reveals a structural mechanism. PLoS Comput Biol. 4:e24.