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@ARTICLE{Schfer:4909,
      author       = {Schäfer, C. and Borm, B. and Born, S. and Möhl, C. and
                      Eibl, E.M. and Hoffmann, B.},
      title        = {{O}ne step ahead: {R}ole of filopodia in adhesion formation
                      during cell migration of keratinocytes},
      journal      = {Experimental cell research},
      volume       = {315},
      issn         = {0014-4827},
      address      = {Orlando, Fla.},
      publisher    = {Academic Press},
      reportid     = {PreJuSER-4909},
      pages        = {1212 - 1224},
      year         = {2009},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Cell adhesion is an essential prerequisite for cell
                      function and movement. It depends strongly on focal adhesion
                      complexes connecting the extracellular matrix to the actin
                      cytoskeleton. Especially in moving cells focal adhesions are
                      highly dynamic and believed to be formed closely behind the
                      leading edge. Filopodia were thought to act mainly as
                      guiding cues using their tip complexes for elongation. Here
                      we show for keratinocytes a strong dependence of
                      lamellipodial adhesion sites on filopodia. Upon stable
                      contact of the VASP-containing tip spot to the substrate, a
                      filopodial focal complex (filopodial FX) is formed right
                      behind along the filopodia axis. These filopodial FXs are
                      fully assembled, yet small adhesions containing all adhesion
                      markers tested. Filopodial FXs when reached by the
                      lamellipodium are just increased in size resulting in
                      classical focal adhesions. At the same time most filopodia
                      regain their elongation ability. Blocking filopodia inhibits
                      development of new focal adhesions in the lamellipodium,
                      while focal adhesion maturation in terms of vinculin
                      exchange dynamics remains active. Our data therefore argue
                      for a strong spatial and temporal dependence of focal
                      adhesions on filopodial focal complexes in keratinocytes
                      with filopodia not permanently initiated via new clustering
                      of actin filaments to induce elongation.},
      keywords     = {Cell Adhesion: physiology / Cell Adhesion Molecules:
                      metabolism / Cell Movement: physiology / Cells, Cultured /
                      Cytoskeletal Proteins: genetics / Cytoskeletal Proteins:
                      metabolism / Fluorescence Recovery After Photobleaching /
                      Focal Adhesions: metabolism / Glycoproteins: genetics /
                      Glycoproteins: metabolism / Humans / Keratinocytes: cytology
                      / Keratinocytes: physiology / Microfilament Proteins:
                      metabolism / Paxillin: genetics / Paxillin: metabolism /
                      Phosphoproteins: metabolism / Pseudopodia: metabolism /
                      Pseudopodia: ultrastructure / Recombinant Fusion Proteins:
                      genetics / Recombinant Fusion Proteins: metabolism / Talin:
                      genetics / Talin: metabolism / Vinculin: genetics /
                      Vinculin: metabolism / Zyxin / Cell Adhesion Molecules (NLM
                      Chemicals) / Cytoskeletal Proteins (NLM Chemicals) /
                      Glycoproteins (NLM Chemicals) / Microfilament Proteins (NLM
                      Chemicals) / Paxillin (NLM Chemicals) / Phosphoproteins (NLM
                      Chemicals) / Recombinant Fusion Proteins (NLM Chemicals) /
                      Talin (NLM Chemicals) / ZYX protein, human (NLM Chemicals) /
                      Zyxin (NLM Chemicals) / vasodilator-stimulated
                      phosphoprotein (NLM Chemicals) / Vinculin (NLM Chemicals) /
                      J (WoSType)},
      cin          = {IBN-4},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB802},
      pnm          = {Kondensierte Materie},
      pid          = {G:(DE-Juel1)FUEK414},
      shelfmark    = {Oncology / Cell Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19100734},
      UT           = {WOS:000265126900012},
      doi          = {10.1016/j.yexcr.2008.11.008},
      url          = {https://juser.fz-juelich.de/record/4909},
}