% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Janotiak:137714,
      author       = {Janoštiak, Radoslav and Brábek, Jan and Auernheimer, Vera
                      and Tatárová, Zuzana and Lautscham, Lena A. and Dey, Tuli
                      and Gemperle, Jakub and Merkel, Rudolf and Goldmann,
                      Wolfgang H. and Fabry, Ben and Rösel, Daniel},
      title        = {{CAS} directly interacts with vinculin to control
                      mechanosensing and focal adhesion dynamics},
      journal      = {Cellular and molecular life sciences},
      volume       = {71},
      number       = {4},
      issn         = {1420-9071},
      address      = {Basel},
      publisher    = {Birkhäuser},
      reportid     = {FZJ-2013-04042},
      pages        = {727-744},
      year         = {2014},
      abstract     = {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},
      cin          = {ICS-7},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-7-20110106},
      pnm          = {453 - Physics of the Cell (POF2-453)},
      pid          = {G:(DE-HGF)POF2-453},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000330586500013},
      doi          = {10.1007/s00018-013-1450-x},
      url          = {https://juser.fz-juelich.de/record/137714},
}