% 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{Kirchenbchler:10586,
      author       = {Kirchenbüchler, D. and Born, S. and Kirchgeßner, N. and
                      Houben, S. and Hoffmann, B. and Merkel, R.},
      title        = {{S}ubstrate, focal adhesion and actin filaments: {A}
                      mechanical unit with a weak spot for mechanosensitive
                      proteins},
      journal      = {Journal of physics / Condensed matter},
      volume       = {22},
      issn         = {0953-8984},
      address      = {Bristol},
      publisher    = {IOP Publ.},
      reportid     = {PreJuSER-10586},
      pages        = {194109},
      year         = {2010},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Mechanosensing is a vital prerequisite for dynamic
                      remodeling of focal adhesions and cytoskeletal structures
                      upon substrate deformation. For example, tissue formation,
                      directed cell orientation or cell differentiation are
                      regulated by such mechanosensing processes. Focal adhesions
                      and the actin cytoskeleton are believed to be involved in
                      these processes, but where mechanosensing molecules are
                      located and how elastic substrate, focal adhesions and the
                      cytoskeleton couple with each other upon substrate
                      deformation still remains obscure. To approach these
                      questions we have developed a sensitive method to apply
                      defined spatially decaying deformation fields to cells
                      cultivated on ultrasoft elastic substrates and to accurately
                      quantify the resulting displacements of the actin
                      cytoskeleton, focal adhesions, as well as the substrate.
                      Displacement fields were recorded in live cell microscopy by
                      tracking either signals from fluorescent proteins or marker
                      particles in the substrate. As model cell type we used
                      myofibroblasts. These cells are characterized by highly
                      stable adhesion and force generating structures but are
                      still able to detect mechanical signals with high
                      sensitivity. We found a rigid connection between substrate
                      and focal adhesions. Furthermore, stress fibers were found
                      to be barely extendable almost over their whole lengths.
                      Plastic deformation took place only at the very ends of
                      actin filaments close to focal adhesions. As a result, this
                      area became elongated without extension of existing actin
                      filaments by polymerization. Both ends of the stress fibers
                      were mechanically coupled with detectable plastic
                      deformations on either site. Interestingly, traction force
                      dependent substrate deformation fields remained mostly
                      unaffected even when stress fiber elongations were released.
                      These data argue for a location of mechanosensing proteins
                      at the ends of actin stress fibers and describe, except for
                      these domains, the whole system to be relatively rigid for
                      tensile strain with a mechanical coupling between the front
                      and rear end of a cell.},
      keywords     = {Actin Cytoskeleton: physiology / Animals / Cell Adhesion:
                      physiology / Cells, Cultured / Fibroblasts: physiology /
                      Intracellular Signaling Peptides and Proteins: physiology /
                      Mechanotransduction, Cellular: physiology / Rats / Rats,
                      Wistar / Intracellular Signaling Peptides and Proteins (NLM
                      Chemicals) / J (WoSType)},
      cin          = {IBN-4},
      ddc          = {530},
      cid          = {I:(DE-Juel1)VDB802},
      pnm          = {BioSoft: Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK505},
      shelfmark    = {Physics, Condensed Matter},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:21386436},
      UT           = {WOS:000277033100012},
      doi          = {10.1088/0953-8984/22/19/194109},
      url          = {https://juser.fz-juelich.de/record/10586},
}