@article{BatsiosIshikawaAnkerholdRothetal.2019,
  author    = {Batsios, Petros and Ishikawa-Ankerhold, Hellen Christina and Roth, Heike and Schleicher, Michael and Wong, Catherine C. L. and M{\"u}ller-Taubenberger, Annette},
  title     = {Ate1-mediated posttranslational arginylation affects substrate adhesion and cell migration in Dictyostelium discoideum},
  series = {Molecular biology of the cell : the official publication of the American Society for Cell Biology},
  volume    = {30},
  journal   = {Molecular biology of the cell : the official publication of the American Society for Cell Biology},
  number    = {4},
  publisher = {American Society for Cell Biology},
  address   = {Bethesda},
  issn      = {1059-1524},
  doi       = {10.1091/mbc.E18-02-0132},
  pages     = {453 -- 466},
  year      = {2019},
  abstract  = {The highly conserved enzyme arginyl-tRNA-protein transferase (Ate1) mediates arginylation, a posttranslational modification that is only incompletely understood at its molecular level. To investigate whether arginylation affects actin-dependent processes in a simple model organism, Dictyostelium discoideum, we knocked out the gene encoding Ate1 and characterized the phenotype of ate1-null cells. Visualization of actin cytoskeleton dynamics by live-cell microscopy indicated significant changes in comparison to wild-type cells. Ate1-null cells were almost completely lacking focal actin adhesion sites at the substrate-attached surface and were only weakly adhesive. In two-dimensional chemotaxis assays toward folate or cAMP, the motility of ate1-null cells was increased. However, in three-dimensional chemotaxis involving more confined conditions, the motility of ate1-null cells was significantly reduced. Live-cell imaging showed that GFP-tagged Ate1 rapidly relocates to sites of newly formed actin-rich protrusions. By mass spectrometric analysis, we identified four arginylation sites in the most abundant actin isoform of Dictyostelium, in addition to arginylation sites in other actin isoforms and several actin-binding proteins. In vitro polymerization assays with actin purified from ate1-null cells revealed a diminished polymerization capacity in comparison to wild-type actin. Our data indicate that arginylation plays a crucial role in the regulation of cytoskeletal activities.},
  language  = {en}
}
@article{SchweigelBatsiosMuellerTaubenbergeretal.2022,
  author    = {Schweigel, Ulrike and Batsios, Petros and M{\"u}ller-Taubenberger, Annette and Gr{\"a}f, Ralph and Grafe, Marianne},
  title     = {Dictyostelium spastin is involved in nuclear envelope dynamics during semi-closed mitosis},
  series = {Nucleus},
  volume    = {13},
  journal   = {Nucleus},
  number    = {1},
  publisher = {Taylor \& Francis Group},
  address   = {Philadelphia},
  issn      = {1949-1034},
  doi       = {10.1080/19491034.2022.2047289},
  pages     = {144 -- 154},
  year      = {2022},
  abstract  = {Dictyostelium amoebae perform a semi-closed mitosis, in which the nuclear envelope is fenestrated at the insertion sites of the mitotic centrosomes and around the central spindle during karyokinesis. During late telophase the centrosome relocates to the cytoplasmic side of the nucleus, the central spindle disassembles and the nuclear fenestrae become closed. Our data indicate that Dictyostelium spastin (DdSpastin) is a microtubule-binding and severing type I membrane protein that plays a role in this process. Its mitotic localization is in agreement with a requirement for the removal of microtubules that would hinder closure of the fenestrae. Furthermore, DdSpastin interacts with the HeH/ LEM-family protein Src1 in BioID analyses as well as the inner nuclear membrane protein Sun1, and shows subcellular co-localizations with Src1, Sun1, the ESCRT component CHMP7 and the IST1-like protein filactin, suggesting that the principal pathway of mitotic nuclear envelope remodeling is conserved between animals and Dictyostelium amoebae.},
  language  = {en}
}