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@ARTICLE{Leber:837684,
      author       = {Leber, Yvonne and Ruparelia, Avnika A. and Kirfel, Gregor
                      and van der Ven, Peter F. M. and Hoffmann, Bernd and Merkel,
                      Rudolf and Bryson-Richardson, Robert J. and Fürst, Dieter
                      O.},
      title        = {{F}ilamin {C} is a highly dynamic protein associated with
                      fast repair of myofibrillar microdamage},
      journal      = {Human molecular genetics},
      volume       = {25},
      number       = {13},
      issn         = {1460-2083},
      address      = {Oxford},
      publisher    = {Oxford Univ. Press},
      reportid     = {FZJ-2017-06546},
      pages        = {2776-2788},
      year         = {2016},
      abstract     = {Filamin c (FLNc) is a large dimeric actin-binding protein
                      located at premyofibrils, myofibrillar Z-discs and
                      myofibrillar attachment sites of striated muscle cells,
                      where it is involved in mechanical stabilization,
                      mechanosensation and intracellular signaling. Mutations in
                      the gene encoding FLNc give rise to skeletal muscle diseases
                      and cardiomyopathies. Here, we demonstrate by fluorescence
                      recovery after photobleaching that a large fraction of FLNc
                      is highly mobile in cultured neonatal mouse cardiomyocytes
                      and in cardiac and skeletal muscles of live transgenic
                      zebrafish embryos. Analysis of cardiomyocytes from Xirp1 and
                      Xirp2 deficient animals indicates that both Xin
                      actin-binding repeat-containing proteins stabilize FLNc
                      selectively in premyofibrils. Using a novel assay to analyze
                      myofibrillar microdamage and subsequent repair in cultured
                      contracting cardiomyocytes by live cell imaging, we
                      demonstrate that repair of damaged myofibrils is achieved
                      within only 4 h, even in the absence of de novo protein
                      synthesis. FLNc is immediately recruited to these sarcomeric
                      lesions together with its binding partner aciculin and
                      precedes detectable assembly of filamentous actin and
                      recruitment of other myofibrillar proteins. These data
                      disclose an unprecedented degree of flexibility of the
                      almost crystalline contractile machinery and imply FLNc as a
                      dynamic signaling hub, rather than a primarily structural
                      protein. Our myofibrillar damage/repair model illustrates
                      how (cardio)myocytes are kept functional in their
                      mechanically and metabolically strained environment. Our
                      results help to better understand the pathomechanisms and
                      pathophysiology of early stages of FLNc-related myofibrillar
                      myopathy and skeletal and cardiac diseases preceding
                      pathological protein aggregation.},
      cin          = {ICS-7},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-7-20110106},
      pnm          = {552 - Engineering Cell Function (POF3-552)},
      pid          = {G:(DE-HGF)POF3-552},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000393064400013},
      pubmed       = {pmid:27206985},
      doi          = {10.1093/hmg/ddw135},
      url          = {https://juser.fz-juelich.de/record/837684},
}