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@ARTICLE{Hudina:1045037,
      author       = {Hudina, Esther and Schott-Verdugo, Stephan and Junglas,
                      Benedikt and Kutzner, Mirka and Ritter, Ilona and Hellmann,
                      Nadja and Schneider, Dirk and Gohlke, Holger and Sachse,
                      Carsten},
      title        = {{T}he bacterial {ESCRT}-{III} {P}sp{A} rods thin lipid
                      tubules and increase membrane curvature through helix α0
                      interactions},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {122},
      number       = {32},
      issn         = {0027-8424},
      address      = {Washington, DC},
      publisher    = {National Acad. of Sciences},
      reportid     = {FZJ-2025-03486},
      pages        = {e2506286122},
      year         = {2025},
      abstract     = {The phage shock protein A (PspA), a bacterial member of the
                      endosomal sorting complexes required for transport
                      (ESCRT)-III superfamily, forms rod-shaped helical assemblies
                      that internalize membrane tubules. The N-terminal helix α0
                      of PspA (and other ESCRT-III members) has been suggested to
                      act as a membrane anchor; the detailed mechanism, however,
                      of how it binds to membranes and eventually triggers
                      membrane fusion and/or fission events remains unclear. By
                      solving a total of 15 cryoelectron microscopy (cryo-EM)
                      structures of PspA and a truncation lacking the N-terminal
                      helix α0 in the presence of Escherichia coli polar lipid
                      membranes, we show in molecular detail how PspA interacts
                      with and remodels membranes: Binding of the N-terminal helix
                      α0 in the outer tubular membrane leaflet induces membrane
                      curvature, supporting membrane tubulation by PspA. Detailed
                      molecular dynamics simulations and free energy computations
                      of interactions between the helix α0 and negatively charged
                      membranes suggest a compensating mechanism between
                      helix-membrane interactions and the energy contributions
                      required for membrane bending. The energetic considerations
                      are in line with the membrane structures observed in the
                      cryo-EM images of tubulated membrane vesicles, fragmented
                      vesicles inside tapered PspA rods, and shedded vesicles
                      emerging at the thinner PspA rod ends. Our results provide
                      insights into the molecular determinants and a potential
                      mechanism of vesicular membrane remodeling mediated by a
                      member of the ESCRT-III superfamily.},
      cin          = {ER-C-3},
      ddc          = {500},
      cid          = {I:(DE-Juel1)ER-C-3-20170113},
      pnm          = {5352 - Understanding the Functionality of Soft Matter and
                      Biomolecular Systems (POF4-535) / 5241 - Molecular
                      Information Processing in Cellular Systems (POF4-524) / SFB
                      1551 R16 - Ein kovalenter und nicht-kovalenter
                      makromolekularer Ansatz zur präzisen und schaltbaren
                      Protein-Oligomerisierung: Grundlegende Einblicke und
                      Kontrolle zellulärer Funktionen (R16#) (549981499)},
      pid          = {G:(DE-HGF)POF4-5352 / G:(DE-HGF)POF4-5241 /
                      G:(GEPRIS)549981499},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {40758888},
      UT           = {WOS:001552219500001},
      doi          = {10.1073/pnas.2506286122},
      url          = {https://juser.fz-juelich.de/record/1045037},
}