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@ARTICLE{Junglas:894346,
      author       = {Junglas, Benedikt and Huber, Stefan T. and Heidler, Thomas
                      and Schlösser, Lukas and Mann, Daniel and Hennig, Raoul and
                      Clarke, Mairi and Hellmann, Nadja and Schneider, Dirk and
                      Sachse, Carsten},
      title        = {{P}sp{A} adopts an {ESCRT}-{III}-like fold and remodels
                      bacterial membranes},
      journal      = {Cell},
      volume       = {184},
      number       = {14},
      issn         = {0092-8674},
      address      = {New York, NY},
      publisher    = {Elsevier},
      reportid     = {FZJ-2021-03192},
      pages        = {3674 - 3688.e18},
      year         = {2021},
      abstract     = {PspA is the main effector of the phage shock protein (Psp)
                      system and preserves the bacterial inner membrane integrity
                      and function. Here, we present the 3.6 Å resolution
                      cryoelectron microscopy (cryo-EM) structure of PspA
                      assembled in helical rods. PspA monomers adopt a canonical
                      ESCRT-III fold in an extended open conformation. PspA rods
                      are capable of enclosing lipids and generating positive
                      membrane curvature. Using cryo-EM, we visualized how PspA
                      remodels membrane vesicles into μm-sized structures and how
                      it mediates the formation of internalized vesicular
                      structures. Hotspots of these activities are zones derived
                      from PspA assemblies, serving as lipid transfer platforms
                      and linking previously separated lipid structures. These
                      membrane fusion and fission activities are in line with the
                      described functional properties of bacterial PspA/IM30/LiaH
                      proteins. Our structural and functional analyses reveal that
                      bacterial PspA belongs to the evolutionary ancestry of
                      ESCRT-III proteins involved in membrane remodeling.},
      cin          = {ER-C-3},
      ddc          = {610},
      cid          = {I:(DE-Juel1)ER-C-3-20170113},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524) / 5352 - Understanding the Functionality of Soft
                      Matter and Biomolecular Systems (POF4-535)},
      pid          = {G:(DE-HGF)POF4-5241 / G:(DE-HGF)POF4-5352},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {34166616},
      UT           = {WOS:000671212300010},
      doi          = {10.1016/j.cell.2021.05.042},
      url          = {https://juser.fz-juelich.de/record/894346},
}