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@ARTICLE{Junglas:1031787,
      author       = {Junglas, Benedikt and Kartte, David and Kutzner, Mirka and
                      Hellmann, Nadja and Ritter, Ilona and Schneider, Dirk and
                      Sachse, Carsten},
      title        = {{S}tructural basis for {V}ipp1 membrane binding: from loose
                      coats and carpets to ring and rod assemblies},
      journal      = {Nature structural $\&$ molecular biology},
      volume       = {32},
      issn         = {1545-9993},
      address      = {London [u.a.]},
      publisher    = {Nature Publishing Group},
      reportid     = {FZJ-2024-05814},
      pages        = {555–570},
      year         = {2025},
      abstract     = {Vesicle-inducing protein in plastids 1 (Vipp1) is critical
                      for thylakoid membrane biogenesis and maintenance. Although
                      Vipp1 has recently been identified as a member of the
                      endosomal sorting complexes required for transport III
                      superfamily, it is still unknown how Vipp1 remodels
                      membranes. Here, we present cryo-electron microscopy
                      structures of Synechocystis Vipp1 interacting with
                      membranes: seven structures of helical and stacked-ring
                      assemblies at 5-7-Å resolution engulfing membranes and
                      three carpet structures covering lipid vesicles at ~20-Å
                      resolution using subtomogram averaging. By analyzing ten
                      structures of N-terminally truncated Vipp1, we show that
                      helix α0 is essential for membrane tubulation and forms the
                      membrane-anchoring domain of Vipp1. Lastly, using a
                      conformation-restrained Vipp1 mutant, we reduced the
                      structural plasticity of Vipp1 and determined two structures
                      of Vipp1 at 3.0-Å resolution, resolving the molecular
                      details of membrane-anchoring and intersubunit contacts of
                      helix α0. Our data reveal membrane curvature-dependent
                      structural transitions from carpets to rings and rods, some
                      of which are capable of inducing and/or stabilizing high
                      local membrane curvature triggering membrane fusion.},
      cin          = {ER-C-3},
      ddc          = {570},
      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)},
      pid          = {G:(DE-HGF)POF4-5352 / G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {39379528},
      UT           = {WOS:001331270100001},
      doi          = {10.1038/s41594-024-01399-z},
      url          = {https://juser.fz-juelich.de/record/1031787},
}