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@ARTICLE{Litschko:860817,
      author       = {Litschko, Christof and Brühmann, Stefan and Csiszár,
                      Agnes and Stephan, Till and Dimchev, Vanessa and
                      Damiano-Guercio, Julia and Junemann, Alexander and Körber,
                      Sarah and Winterhoff, Moritz and Nordholz, Benjamin and
                      Ramalingam, Nagendran and Peckham, Michelle and Rottner,
                      Klemens and Merkel, Rudolf and Faix, Jan},
      title        = {{F}unctional integrity of the contractile actin cortex is
                      safeguarded by multiple {D}iaphanous-related formins},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {116},
      number       = {9},
      issn         = {1091-6490},
      address      = {Washington, DC},
      publisher    = {National Acad. of Sciences},
      reportid     = {FZJ-2019-01472},
      pages        = {3594-3603},
      year         = {2019},
      abstract     = {The contractile actin cortex is a thin layer of filamentous
                      actin, myosin motors, and regulatory proteins beneath the
                      plasma membrane crucial to cytokinesis, morphogenesis, and
                      cell migration. However, the factors regulating actin
                      assembly in this compartment are not well understood. Using
                      the Dictyostelium model system, we show that the three
                      Diaphanous-related formins (DRFs) ForA, ForE, and ForH are
                      regulated by the RhoA-like GTPase RacE and synergize in the
                      assembly of filaments in the actin cortex. Single or double
                      formin-null mutants displayed only moderate defects in
                      cortex function whereas the concurrent elimination of all
                      three formins or of RacE caused massive defects in cortical
                      rigidity and architecture as assessed by aspiration assays
                      and electron microscopy. Consistently, the triple formin and
                      RacE mutants encompassed large peripheral patches devoid of
                      cortical F-actin and exhibited severe defects in cytokinesis
                      and multicellular development. Unexpectedly, many
                      forA−/E−/H− and racE− mutants protruded efficiently,
                      formed multiple exaggerated fronts, and migrated with
                      morphologies reminiscent of rapidly moving fish keratocytes.
                      In 2D-confinement, however, these mutants failed to properly
                      polarize and recruit myosin II to the cell rear essential
                      for migration. Cells arrested in these conditions displayed
                      dramatically amplified flow of cortical actin filaments, as
                      revealed by total internal reflection fluorescence (TIRF)
                      imaging and iterative particle image velocimetry (PIV).
                      Consistently, individual and combined, CRISPR/Cas9-mediated
                      disruption of genes encoding mDia1 and -3 formins in B16-F1
                      mouse melanoma cells revealed enhanced frequency of cells
                      displaying multiple fronts, again accompanied by defects in
                      cell polarization and migration. These results suggest
                      evolutionarily conserved functions for formin-mediated actin
                      assembly in actin cortex mechanics.},
      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},
      pubmed       = {pmid:30808751},
      UT           = {WOS:000459694400044},
      doi          = {10.1073/pnas.1821638116},
      url          = {https://juser.fz-juelich.de/record/860817},
}