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@ARTICLE{Mann:1019308,
      author       = {Mann, Daniel and Fromm, Simon A. and Martinez-Sanchez,
                      Antonio and Gopaldass, Navin and Choy, Ramona and Mayer,
                      Andreas and Sachse, Carsten},
      title        = {{A}tg18 oligomer organization in assembled tubes and on
                      lipid membrane scaffolds},
      journal      = {Nature Communications},
      volume       = {14},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {FZJ-2023-05282},
      pages        = {8086},
      year         = {2023},
      abstract     = {Autophagy-related protein 18 (Atg18) participates in the
                      elongation of early autophagosomal structures in concert
                      with Atg2 and Atg9 complexes. How Atg18 contributes to the
                      structural coordination of Atg2 and Atg9 at the isolation
                      membrane remains to be understood. Here, we determined the
                      cryo-EM structures of Atg18 organized in helical tubes,
                      Atg18 oligomers in solution as well as on lipid membrane
                      scaffolds. The helical assembly is composed of Atg18
                      tetramers forming a lozenge cylindrical lattice with
                      remarkable structural similarity to the COPII outer coat.
                      When reconstituted with lipid membranes, using subtomogram
                      averaging we determined tilted Atg18 dimer structures
                      bridging two juxtaposed lipid membranes spaced apart by 80
                      Å. Moreover, lipid reconstitution experiments further
                      delineate the contributions of Atg18's FRRG motif and the
                      amphipathic helical extension in membrane interaction. The
                      observed structural plasticity of Atg18's oligomeric
                      organization and membrane binding properties provide a
                      molecular framework for the positioning of downstream
                      components of the autophagy machinery.},
      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)},
      pid          = {G:(DE-HGF)POF4-5352 / G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {38057304},
      UT           = {WOS:001135959900008},
      doi          = {10.1038/s41467-023-43460-3},
      url          = {https://juser.fz-juelich.de/record/1019308},
}