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@ARTICLE{Niediek:21272,
      author       = {Niediek, V. and Born, S. and Hampe, N. and Kirchgeßne, N.
                      and Merkel, R. and Hoffmann, B.},
      title        = {{C}yclic {S}tretch induces reorientation of cells in a
                      {S}rc family kinase and p130{C}as dependent manner},
      journal      = {European Journal of Cell Biology},
      volume       = {91},
      issn         = {1618-1298},
      address      = {München},
      publisher    = {Elsevier},
      reportid     = {PreJuSER-21272},
      pages        = {118 - 128},
      year         = {2012},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Recognition of external mechanical signals by cells is an
                      essential process for life. One important mechanical signal
                      experienced by various cell types, e.g. around blood
                      vessels, within the lung epithelia or around the intestine,
                      is cyclic stretch. As a response, many cell types reorient
                      their actin cytoskeleton and main cell axis almost
                      perpendicular to the direction of stretch. Despite the vital
                      necessity of cellular adaptation to cyclic stretch, the
                      underlying mechanosensory signal cascades are far from being
                      understood. Here we show an important function of Src-family
                      kinase activity in cellular reorientation upon cyclic
                      stretch. Deletion of all three family members, namely c-Src,
                      Yes and Fyn (SYF), results in a strongly impaired cell
                      reorientation of mouse embryonic fibroblasts with an only
                      incomplete reorientation upon expression of c-Src. We
                      further demonstrate that this reorientation phenotype of
                      SYF-depleted cells is not caused by affected protein
                      exchange dynamics within focal adhesions or altered cell
                      force generation. Instead, Src-family kinases regulate the
                      reorientation in a mechanotransduction-dependent manner,
                      since knock-down and knock-out of p130Cas, a putative
                      stretch sensor known to be phosphorylated by Src-family
                      kinases, also reduce cellular reorientation upon cyclic
                      stretch. This impaired reorientation is identical in
                      intensity upon mutating stretch-sensitive tyrosines of
                      p130Cas only. These statistically highly significant data
                      pinpoint early events in a Src family kinase- and
                      p130Cas-dependent mechanosensory/mechanotransduction
                      pathway.},
      keywords     = {Animals / Cell Movement / Cells, Cultured / Crk-Associated
                      Substrate Protein: genetics / Crk-Associated Substrate
                      Protein: metabolism / Fibroblasts: drug effects /
                      Fibroblasts: physiology / Focal Adhesions / Gene Knockout
                      Techniques / Mechanotransduction, Cellular / Mice /
                      Phosphorylation / Proto-Oncogene Proteins c-fyn: genetics /
                      Proto-Oncogene Proteins c-yes: genetics / Pyrazoles:
                      pharmacology / Pyrimidines: pharmacology / RNA, Small
                      Interfering: genetics / Stress, Mechanical / Transfection /
                      src-Family Kinases: antagonists $\&$ inhibitors / src-Family
                      Kinases: genetics / src-Family Kinases: metabolism /
                      4-amino-7-phenylpyrazol(3,4-d)pyrimidine (NLM Chemicals) /
                      AG 1879 (NLM Chemicals) / Crk-Associated Substrate Protein
                      (NLM Chemicals) / Pyrazoles (NLM Chemicals) / Pyrimidines
                      (NLM Chemicals) / RNA, Small Interfering (NLM Chemicals) /
                      Proto-Oncogene Proteins c-yes (NLM Chemicals) / Fyn protein,
                      mouse (NLM Chemicals) / Proto-Oncogene Proteins c-fyn (NLM
                      Chemicals) / Yes1 protein, mouse (NLM Chemicals) /
                      src-Family Kinases (NLM Chemicals) / J (WoSType)},
      cin          = {ICS-7},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-7-20110106},
      pnm          = {BioSoft: Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK505},
      shelfmark    = {Cell Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22178114},
      UT           = {WOS:000301095900003},
      doi          = {10.1016/j.ejcb.2011.10.003},
      url          = {https://juser.fz-juelich.de/record/21272},
}