Dimerization and direct membrane interaction of Nup53 contribute to nuclear pore complex assembly.
Copyright policy )Dimerization and direct membrane interaction of Nup53 contribute to nuclear pore complex assembly.
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.
Binding Sites, Saccharomyces cerevisiae Proteins, Molecular Sequence Data, Xenopus Proteins, Membrane Fusion, Article, Protein Structure, Tertiary, Nuclear Pore Complex Proteins, Structure-Activity Relationship, Xenopus laevis, Liposomes, Mutagenesis, Site-Directed, Nuclear Pore, Animals, Humans, Amino Acid Sequence, Dimerization, Interphase, Conserved Sequence, HeLa Cells, Protein Binding
Binding Sites, Saccharomyces cerevisiae Proteins, Molecular Sequence Data, Xenopus Proteins, Membrane Fusion, Article, Protein Structure, Tertiary, Nuclear Pore Complex Proteins, Structure-Activity Relationship, Xenopus laevis, Liposomes, Mutagenesis, Site-Directed, Nuclear Pore, Animals, Humans, Amino Acid Sequence, Dimerization, Interphase, Conserved Sequence, HeLa Cells, Protein Binding
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