title: Dimerization and direct membrane interaction of Nup53 contribute to nuclear pore complex assembly.
abstract: Nuclear pore complexes (NPCs) fuse the two membranes of the nuclear envelope (NE) to a pore, connecting cytoplasm and nucleoplasm and allowing exchange of macromolecules between these compartments. Most NPC proteins do not contain integral membrane domains and thus it is largely unclear how NPCs are embedded and anchored in the NE. Here, we show that the evolutionary conserved nuclear pore protein Nup53 binds independently of other proteins to membranes, a property that is crucial for NPC assembly and conserved between yeast and vertebrates. The vertebrate protein comprises two membrane binding sites, of which the C-terminal domain has membrane deforming capabilities, and is specifically required for de novo NPC assembly and insertion into the intact NE during interphase. Dimerization of Nup53 contributes to its membrane interaction and is crucial for its function in NPC assembly.
authors.affiliation: Friedrich Miescher Laboratory of the Max Planck Society, Tübingen, Germany.
authors.forename: Benjamin
authors.initials: B
authors.lastname: Vollmer
authors.forename: Allana
authors.initials: A
authors.lastname: Schooley
authors.forename: Ruchika
authors.initials: R
authors.lastname: Sachdev
authors.forename: Nathalie
authors.initials: N
authors.lastname: Eisenhardt
authors.forename: Anna M
authors.initials: AM
authors.lastname: Schneider
authors.forename: Cornelia
authors.initials: C
authors.lastname: Sieverding
authors.forename: Johannes
authors.initials: J
authors.lastname: Madlung
authors.forename: Uwe
authors.initials: U
authors.lastname: Gerken
authors.forename: Boris
authors.initials: B
authors.lastname: Macek
authors.forename: Wolfram
authors.initials: W
authors.lastname: Antonin
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D017124:Conserved Sequence; D019281:Dimerization; D006367:HeLa Cells; D006801:Humans; D007399:Interphase; D008081:Liposomes; D008561:Membrane Fusion; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D022022:Nuclear Pore / Q000378:metabolism* / Q000648:ultrastructure; D028861:Nuclear Pore Complex Proteins / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism; D013329:Structure-Activity Relationship; D029867:Xenopus Proteins / Q000737:chemistry / Q000378:metabolism*; D014982:Xenopus laevis
chemical_list: C116844:ASM4 protein, S cerevisiae; D008081:Liposomes; C116843:NUP53 protein, S cerevisiae; D028861:Nuclear Pore Complex Proteins; C577342:Nup53 protein, Xenopus laevis; D029701:Saccharomyces cerevisiae Proteins; D029867:Xenopus Proteins