% 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{Kpper:14490,
      author       = {Küpper, K. and Lang, N. and Möhl, C. and Kirchgeßner, N.
                      and Born, S. and Goldmann, W.H. and Hoffmann, B. and Merkel,
                      R.},
      title        = {{T}yrosine phosphorylation of vinculin at position 1065
                      modifies focal adhesion dynamics and cell tractions},
      journal      = {Biochemical and biophysical research communications},
      volume       = {399},
      issn         = {0006-291X},
      address      = {Orlando, Fla.},
      publisher    = {Academic Press},
      reportid     = {PreJuSER-14490},
      pages        = {560 - 564},
      year         = {2010},
      note         = {We thank Dr. E.D. Adamson for providing the MEF cells and
                      Dr. B. Fabry for stimulating discussions. We are also
                      indebted to the entire team of IBN 4 for their interlectual
                      input. This work was supported by grants from
                      Bayerisch-Franzosisches Hochschulzentrum, Deutscher
                      Akademischer Austausch Dienst, Bavaria California Technology
                      Center, Deutsche Forschungsgemeinschaft (G0598/13-1), and
                      Bundesministerium fur Bildung und Forschung (Program
                      0315501).},
      abstract     = {Focal adhesions (FAs) connect the cellular actin
                      cytoskeleton via integrin with the extracellular matrix.
                      They comprise of many structural and signaling proteins
                      which are highly dynamic, well regulated, and responsible
                      for the sensing of physical properties from the environment.
                      Vinculin is a protein that incorporates all these functions.
                      Here, we investigated the phosphorylation of Y1065 in the
                      activation/regulation of vinculin. We used different
                      vinculin mutants mimicking either a permanently activated or
                      inhibited phosphorylation site at position 1065. Using these
                      mutants, we determined their influence on the exchange
                      dynamics and cell forces using fluorescence recovery after
                      photobleaching and traction microscopy. The results indicate
                      that phosphorylation at Y1065 significantly increases the
                      amount of freely exchanging vinculin within FAs whereas
                      inhibition of this phosphorylation site leads to an
                      uncontrolled exchange of vinculin and reduced adhesive cell
                      forces. In conclusion, we show that phosphorylation on
                      position Y1065 is essential for accurate incorporation of
                      vinculin into FAs and mechanical behavior of cells.},
      keywords     = {Animals / Focal Adhesions: genetics / Focal Adhesions:
                      metabolism / Mice / Mice, Knockout / Mutation /
                      Phosphorylation / Tyrosine: genetics / Tyrosine: metabolism
                      / Vinculin: genetics / Vinculin: metabolism / Vinculin (NLM
                      Chemicals) / Tyrosine (NLM Chemicals) / J (WoSType)},
      cin          = {IBN-4},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB802},
      pnm          = {BioSoft: Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK505},
      shelfmark    = {Biochemistry $\&$ Molecular Biology / Biophysics},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:20678470},
      UT           = {WOS:000281840200017},
      doi          = {10.1016/j.bbrc.2010.07.110},
      url          = {https://juser.fz-juelich.de/record/14490},
}