% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Schlsser:1048414,
      author       = {Schlösser, Lukas and Kutzner, Mirka and Hellmann, Nadja
                      and Kiesewetter, Denis and Bieber, Julia and Quarta, Ndjali
                      and Ge, Xingwu and Goetze, Tom and Junglas, Benedikt and
                      Matsumura, Fumiki and Bonn, Mischa and Gräter, Frauke and
                      Sachse, Carsten and Liu, Lu-Ning and Schmidt, Carla and
                      Aponte-Santamaría, Camilo and Schneider, Dirk},
      title        = {{M}embrane binding of a cyanobacterial {ESCRT} ‐ {III}
                      protein crucially involves the helix α 1‐3 hairpin
                      conserved in all superfamily members},
      journal      = {Protein science},
      volume       = {34},
      number       = {12},
      issn         = {0961-8368},
      address      = {Hoboken, NJ},
      publisher    = {Wiley},
      reportid     = {FZJ-2025-04625},
      pages        = {e70387},
      year         = {2025},
      abstract     = {IM30, the inner membrane-associated protein of 30 kDa (also
                      known as Vipp1) is essential for thylakoid membrane
                      biogenesis and/or maintenance in chloroplasts and
                      cyanobacteria. IM30 and its bacterial homolog PspA belong to
                      the ESCRT-III superfamily, proteins previously thought to be
                      restricted to eukaryotes and archaea. Despite low sequence
                      similarity, IM30 shares key structural and functional
                      features with eukaryotic ESCRT-IIIs, including a conserved
                      α1-α2 helical hairpin core and the ability to form
                      oligomeric barrel or rod assemblies that mediate membrane
                      remodeling. Using IM30 variants, we now show that membrane
                      binding of IM30 is driven by electrostatic interactions
                      between the positively charged α1-α3 helical hairpin and
                      negatively charged lipid surfaces, paralleling the role of
                      charged helical regions in some eukaryotic ESCRT-IIIs. This
                      likely is followed by lateral assembly of IM30 into
                      higher-order barrel or rod structures on the membrane. Once
                      assembled, α0 helices within these oligomers engage and
                      stabilize internalized membrane tubules, mirroring membrane
                      interaction strategies of eukaryotic ESCRT-IIIs, which use
                      both N-terminal sequence motifs and charged residues on
                      α1/α2. Thus, our findings demonstrate a conserved membrane
                      binding and remodeling mechanism across the ESCRT-III
                      superfamily, underscoring an evolutionary link in membrane
                      dynamics between pro- and eukaryotes.},
      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},
      doi          = {10.1002/pro.70387},
      url          = {https://juser.fz-juelich.de/record/1048414},
}