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Atg18 oligomer organization in assembled tubes and on lipid membrane scaffolds

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dc.contributor.authorMann, Daniel
dc.contributor.authorFromm, Simon
dc.contributor.authorMartinez-Sanchez, Antonio
dc.contributor.authorGopaldass, Navin
dc.contributor.authorChoy, Ramona
dc.contributor.authorMayer, Andreas
dc.contributor.authorSachse, Carsten
dc.contributor.departmentIngeniería de la Información y las Comunicaciones
dc.date.accessioned2023-12-20T11:20:48Z
dc.date.available2023-12-20T11:20:48Z
dc.date.issued2023-12-06
dc.description© 2023. The authors. This document is made available under the CC-BY 4.0 license http://creativecommons.org/licenses/by /4.0/ This document is the submitted/accepted/ published version of a published Work that appeared in final form in Nature Comminications. To access the final edited and published work see https://doi.org/10.1038/s41467-023-43460-3es
dc.description.abstractAutophagy-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.es
dc.formatapplication/pdfes
dc.formatvideo/mp4es
dc.format.extent13es
dc.identifier.citationNature Communications 14, 8086 (2023)
dc.identifier.doihttps://doi.org/10.1038/s41467-023-43460-3
dc.identifier.issn2041-1723
dc.identifier.urihttp://hdl.handle.net/10201/136778
dc.languageenges
dc.publisherElsevieres
dc.relationOpen Access funding enabled and organized by Projekt DEAL.es
dc.relation.publisherversionhttps://www.nature.com/articles/s41467-023-43460-3es
dc.rightsinfo:eu-repo/semantics/openAccesses
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.titleAtg18 oligomer organization in assembled tubes and on lipid membrane scaffoldses
dc.typeinfo:eu-repo/semantics/articlees
dspace.entity.typePublicationes
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