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@ARTICLE{Huber:877662,
      author       = {Huber, Stefan T. and Mostafavi, Siavash and Mortensen,
                      Simon and Sachse, Carsten},
      title        = {{S}tructure and assembly of {ESCRT}-{III} helical {V}ps24
                      filaments},
      journal      = {Science advances},
      volume       = {6},
      number       = {34},
      issn         = {2375-2548},
      address      = {Washington, DC [u.a.]},
      publisher    = {Assoc.},
      reportid     = {FZJ-2020-02372},
      pages        = {eaba4897 -},
      year         = {2020},
      abstract     = {ESCRT-III proteins mediate a range of cellular membrane
                      remodeling activities such as multivesicular body
                      biogenesis, cytokinesis, and viral release. Critical to
                      these processes is the assembly of ESCRT-III subunits into
                      polymeric structures. In this study, we determined the
                      cryo-EM structure of a helical assembly of Saccharomyces
                      cerevisiae Vps24 at 3.2-Å resolution and found that Vps24
                      adopts an elongated open conformation. Vps24 forms a
                      domain-swapped dimer extended into protofilaments that
                      associate into a double-stranded apolar filament. We
                      demonstrate that, upon binding negatively charged lipids,
                      Vps24 homopolymer filaments undergo partial disassembly into
                      shorter filament fragments and oligomers. Upon the addition
                      of Vps24, Vps2, and Snf7, liposomes are deformed into neck
                      and tubular structures by an ESCRT-III heteropolymer coat.
                      The filamentous Vps24 homopolymer assembly structure and
                      interaction studies reveal how Vps24 could introduce unique
                      geometric properties to mixed-type ESCRT-III heteropolymers
                      and contribute to the process of membrane scission events.},
      cin          = {ER-C-3},
      ddc          = {500},
      cid          = {I:(DE-Juel1)ER-C-3-20170113},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32875105},
      UT           = {WOS:000561426700011},
      doi          = {10.1126/sciadv.aba4897},
      url          = {https://juser.fz-juelich.de/record/877662},
}