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dc.contributor.authorKralt, Annemarie
dc.contributor.authorWojtynek, Matthias
dc.contributor.authorFischer, Jonas S.
dc.contributor.authorAgote-Aran, Arantxa
dc.contributor.authorMancini, Roberta
dc.contributor.authorDultz, Elisa
dc.contributor.authorNoor, Elad
dc.contributor.authorUliana, Federico
dc.contributor.authorTatarek-Nossol, Marianna
dc.contributor.authorAntonin, Wolfram
dc.contributor.authorOnishchenko, Evgeny
dc.contributor.authorMedalia, Ohad
dc.contributor.authorWeis, Karsten
dc.description.abstractThe nuclear pore complex (NPC) is the central portal for macromolecular exchange between the nucleus and cytoplasm. In all eukaryotes, NPCs assemble into an intact nuclear envelope (NE) during interphase, but the process of NPC biogenesis remains poorly characterized. Furthermore, little is known about how NPC assembly leads to the fusion of the outer and inner NE, and no factors have been identified that could trigger this event. Here, we characterize the transmembrane protein Brl1 as an NPC assembly factor required for NE fusion in budding yeast. Brl1 preferentially associates with NPC assembly intermediates and its depletion halts NPC biogenesis, leading to NE herniations that contain inner and outer ring nucleoporins but lack the cytoplasmic export platform. Furthermore, we identify an essential amphipathic helix in the luminal domain of Brl1 that mediates interactions with lipid bilayers. Mutations in this amphipathic helix lead to NPC assembly defects, and cryo-electron tomography analyses reveal multilayered herniations of the inner nuclear membrane with NPC-like structures at the neck, indicating a failure in NE fusion. Taken together, our results identify a role for Brl1 in NPC assembly and suggest a function of its amphipathic helix in mediating the fusion of the inner and outer nuclear membranes.en_US
dc.publishereLife Sciences Publicationsen_US
dc.rightsNavngivelse 4.0 Internasjonal*
dc.titleAn amphipathic helix in Brl1 is required for nuclear pore complex biogenesis in S. cerevisiaeen_US
dc.typeJournal articleen_US
dc.typePeer revieweden_US
dc.rights.holderCopyright 2022 the authorsen_US
dc.identifier.citationeLIFE. 2022, 11, e78385.en_US

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Navngivelse 4.0 Internasjonal
Except where otherwise noted, this item's license is described as Navngivelse 4.0 Internasjonal