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@ARTICLE{Mhl:4910,
      author       = {Möhl, C. and Kirchgeßner, N. and Schäfer, C. and
                      Küpper, K. and Born, S. and Diez, G. and Goldmann, W.H. and
                      Merkel, R. and Hoffmann, B.},
      title        = {{B}ecoming {S}table and {S}trong: {T}he {I}nterplay between
                      {V}inculin {E}xchange {D}ynamics and {A}dhesion {S}trength
                      {D}uring {A}dhesion {S}ite {M}aturation},
      journal      = {Cell Motility and the Cytoskeleton},
      volume       = {66},
      issn         = {0886-1544},
      address      = {Bognor Regis},
      publisher    = {Wiley},
      reportid     = {PreJuSER-4910},
      pages        = {350 - 364},
      year         = {2009},
      note         = {Contract grant sponsors: BFHZ, BaCaTec, and DAAD.},
      abstract     = {The coordinated formation and release of focal adhesions is
                      necessary for cell attachment and migration. According to
                      current models, these processes are caused by temporal
                      variations in protein composition. Protein incorporation
                      into focal adhesions is believed to be controlled by
                      phosphorylation. Here, we tested the exchange dynamics of
                      GFP-vinculin as marker protein of focal adhesions using the
                      method of Fluorescence Recovery After Photobleaching. The
                      relevance of the phosphorylation state of the protein, the
                      age of focal adhesions and the acting force were
                      investigated. For stable focal adhesions of stationary
                      keratinocytes, we determined an exchangeable vinculin
                      fraction of $52\%$ and a recovery halftime of 57 s. Nascent
                      focal adhesions of moving cells contained a fraction of
                      exchanging vinculin of $70\%$ with a recovery halftime of 36
                      s. Upon maturation, mean saturation values and recovery
                      halftimes decreased to levels of $49\%$ and 42 s,
                      respectively. Additionally, the fraction of stably
                      incorporated vinculin increased with cell forces and
                      decreased with vinculin phosphorylation within these sites.
                      Experiments on a nonphosphorylatable vinculin mutant
                      construct at phosphorylation site tyr1065 confirmed the
                      direct interplay between phosphorylation and exchange
                      dynamics of adhesion proteins during adhesion site
                      maturation.},
      keywords     = {Cell Adhesion: physiology / Cell Movement: physiology /
                      Cells, Cultured / Fluorescence Recovery After Photobleaching
                      / Focal Adhesions: metabolism / Humans / Keratinocytes:
                      cytology / Keratinocytes: metabolism / Phosphorylation:
                      physiology / Vinculin: genetics / Vinculin: metabolism /
                      Vinculin (NLM Chemicals) / J (WoSType)},
      cin          = {IBN-4},
      ddc          = {590},
      cid          = {I:(DE-Juel1)VDB802},
      pnm          = {Kondensierte Materie},
      pid          = {G:(DE-Juel1)FUEK414},
      shelfmark    = {Cell Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19422016},
      UT           = {WOS:000266466700005},
      doi          = {10.1002/cm.20375},
      url          = {https://juser.fz-juelich.de/record/4910},
}