@phdthesis{GeisenhofgebTrinkwalder2019,
  author    = {Geisenhof [geb. Trinkwalder], Michaela},
  title     = {Erforschung des Schicksals des Mittelk{\"o}rpers anhand der ZF1-Methode},
  doi       = {10.25972/OPUS-18219},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-182199},
  school      = {Universit{\"a}t W{\"u}rzburg},
  year      = {2019},
  abstract  = {Bei der Teilung einer Zelle werden das Genom und die Zellbestandteile zwischen zwei Tochterzellen aufgeteilt. Dies erfordert verschiedene fein aufeinander abgestimmte Vorg{\"a}nge. Unter anderem ist eine proteinreiche Struktur beteiligt, die 1891 entdeckt wurde: der Mittelk{\"o}rper. In vorliegender Arbeit wurden gezielt gekennzeichnete Mittelk{\"o}rperproteine analysiert und verschiedene Phasen des Transports unterschieden. Es erfolgten erstmals Messungen unter Nutzung der ZF1-Methode. Zudem wird anhand der ZF1-Technik nachgewiesen, dass im Rahmen der Zellteilung die Trennung der interzellul{\"a}ren Br{\"u}cke zu beiden Seiten des Mittelk{\"o}rpers stattfindet, woraufhin dieser nach extrazellul{\"a}r abgegeben wird und {\"u}ber einen der Phagozytose {\"a}hnlichen und von Aktin abh{\"a}ngigen Mechanismus von einer Tochterzelle oder unverwandten Nachbarzelle aufgenommen wird.},
  subject      = {Mitose},
  language  = {de}
}
@article{FazeliBeerGeisenhofetal.2020,
  author    = {Fazeli, Gholamreza and Beer, Katharina B. and Geisenhof, Michaela and Tr{\"o}ger, Sarah and K{\"o}nig, Julia and M{\"u}ller-Reichert, Thomas and Wehman, Ann M.},
  title     = {Loss of the Major Phosphatidylserine or Phosphatidylethanolamine Flippases Differentially Affect Phagocytosis},
  series = {Frontiers in Cell and Developmental Biology},
  volume    = {8},
  journal   = {Frontiers in Cell and Developmental Biology},
  issn      = {2296-634X},
  doi       = {10.3389/fcell.2020.00648},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-208771},
  year      = {2020},
  abstract  = {The lipids phosphatidylserine (PtdSer) and phosphatidylethanolamine (PtdEth) are normally asymmetrically localized to the cytosolic face of membrane bilayers, but can both be externalized during diverse biological processes, including cell division, cell fusion, and cell death. Externalized lipids in the plasma membrane are recognized by lipid-binding proteins to regulate the clearance of cell corpses and other cell debris. However, it is unclear whether PtdSer and PtdEth contribute in similar or distinct ways to these processes. We discovered that disruption of the lipid flippases that maintain PtdSer or PtdEth asymmetry in the plasma membrane have opposite effects on phagocytosis in Caenorhabditis elegans embryos. Constitutive PtdSer externalization caused by disruption of the major PtdSer flippase TAT-1 led to increased phagocytosis of cell debris, sometimes leading to two cells engulfing the same debris. In contrast, PtdEth externalization caused by depletion of the major PtdEth flippase TAT-5 or its activator PAD-1 disrupted phagocytosis. These data suggest that PtdSer and PtdEth externalization have opposite effects on phagocytosis. Furthermore, externalizing PtdEth is associated with increased extracellular vesicle release, and we present evidence that the extent of extracellular vesicle accumulation correlates with the extent of phagocytic defects. Thus, a general loss of lipid asymmetry can have opposing impacts through different lipid subtypes simultaneously exerting disparate effects.},
  language  = {en}
}