TY  - JOUR
AU  - Janoštiak, Radoslav
AU  - Brábek, Jan
AU  - Auernheimer, Vera
AU  - Tatárová, Zuzana
AU  - Lautscham, Lena A.
AU  - Dey, Tuli
AU  - Gemperle, Jakub
AU  - Merkel, Rudolf
AU  - Goldmann, Wolfgang H.
AU  - Fabry, Ben
AU  - Rösel, Daniel
TI  - CAS directly interacts with vinculin to control mechanosensing and focal adhesion dynamics
JO  - Cellular and molecular life sciences
VL  - 71
IS  - 4
SN  - 1420-9071
CY  - Basel
PB  - Birkhäuser
M1  - FZJ-2013-04042
SP  - 727-744
PY  - 2014
AB  - Focal adhesions are cellular structures through which both mechanical forces and regulatory signals are transmitted. Two focal adhesion-associated proteins, Crk-associated substrate (CAS) and vinculin, were both independently shown to be crucial for the ability of cells to transmit mechanical forces and to regulate cytoskeletal tension. Here, we identify a novel, direct binding interaction between CAS and vinculin. This interaction is mediated by the CAS SRC homology 3 domain and a proline-rich sequence in the hinge region of vinculin. We show that CAS localization in focal adhesions is partially dependent on vinculin, and that CAS–vinculin coupling is required for stretch-induced activation of CAS at the Y410 phosphorylation site. Moreover, CAS–vinculin binding significantly affects the dynamics of CAS and vinculin within focal adhesions as well as the size of focal adhesions. Finally, disruption of CAS binding to vinculin reduces cell stiffness and traction force generation. Taken together, these findings strongly implicate a crucial role of CAS–vinculin interaction in mechanosensing and focal adhesion dynamics
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000330586500013
DO  - DOI:10.1007/s00018-013-1450-x
UR  - https://juser.fz-juelich.de/record/137714
ER  -