% 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{Moch:811941,
      author       = {Moch, Marcin and Windoffer, Reinhard and Schwarz, Nicole
                      and Pohl, Raphaela and Omenzetter, Andreas and Schnakenberg,
                      Uwe and Herb, Fabian and Chaisaowong, Kraisorn and Merhof,
                      Dorit and Ramms, Lena and Fabris, Gloria and Hoffmann, Bernd
                      and Merkel, Rudolf and Leube, Rudolf E.},
      title        = {{E}ffects of {P}lectin {D}epletion on {K}eratin {N}etwork
                      {D}ynamics and {O}rganization},
      journal      = {PLoS one},
      volume       = {11},
      number       = {3},
      issn         = {1932-6203},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {FZJ-2016-04251},
      pages        = {e0149106 -},
      year         = {2016},
      abstract     = {The keratin intermediate filament cytoskeleton protects
                      epithelial cells against various types of stress and is
                      involved in fundamental cellular processes such as
                      signaling, differentiation and organelle trafficking. These
                      functions rely on the cell type-specific arrangement and
                      plasticity of the keratin system. It has been suggested that
                      these properties are regulated by a complex cycle of
                      assembly and disassembly. The exact mechanisms responsible
                      for the underlying molecular processes, however, have not
                      been clarified. Accumulating evidence implicates the
                      cytolinker plectin in various aspects of the keratin cycle,
                      i.e., by acting as a stabilizing anchor at hemidesmosomal
                      adhesion sites and the nucleus, by affecting keratin
                      bundling and branching and by linkage of keratins to actin
                      filament and microtubule dynamics. In the present study we
                      tested these hypotheses. To this end, plectin was
                      downregulated by shRNA in vulvar carcinoma-derived A431
                      cells. As expected, integrin β4- and BPAG-1-positive
                      hemidesmosomal structures were strongly reduced and
                      cytosolic actin stress fibers were increased. In addition,
                      integrins α3 and β1 were reduced. The experiments
                      furthermore showed that loss of plectin led to a reduction
                      in keratin filament branch length but did not alter overall
                      mechanical properties as assessed by indentation analyses
                      using atomic force microscopy and by displacement analyses
                      of cytoplasmic superparamagnetic beads using magnetic
                      tweezers. An increase in keratin movement was observed in
                      plectin-depleted cells as was the case in control cells
                      lacking hemidesmosome-like structures. Yet, keratin turnover
                      was not significantly affected. We conclude that plectin
                      alone is not needed for keratin assembly and disassembly and
                      that other mechanisms exist to guarantee proper keratin
                      cycling under steady state conditions in cultured single
                      cells.},
      cin          = {ICS-7},
      ddc          = {500},
      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:000372701200017},
      doi          = {10.1371/journal.pone.0149106},
      url          = {https://juser.fz-juelich.de/record/811941},
}