Dimerization and direct membrane interaction of Nup53 contribute to nuclear pore complex assembly
Open accessAbstract
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.
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Nup35 associates with Nup155 early during NPC assembly.
“Since Nup35 associates with Nup155 early during NPC assembly (39), its dimerizing domain appears critical to scaffold its flexible linkers towards neighboring spokes within IR membrane coat.”
From AI-based structure prediction empowers integrative structural analysis of human nuclear pores (2022) · cites this paper as [39]
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- Authors
- Vollmer, B., Schooley, A., Sachdev, R., Eisenhardt, N., Schneider, A. M., Sieverding, C., Madlung, J., Gerken, U., Macek, B., & Antonin, W.
- Affiliations
- Max Planck Society (DE)
- Max Planck Institute for Developmental Biology (DE)
- University of Tübingen (DE)
- University of Hohenheim (DE)
- Corresponding author
- Antonin, Wolfram
- Venue
- The EMBO Journal
- Published
- 2012-09-07
- Volume
- 31
- Issue
- 20
- Pages
- 4072-4084
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC3474928
- OpenAlex
- W2152318348
- Cited by
- 104
- References
- 64
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 3 · 2023: 13 · 2022: 11 · 2021: 11 · 2020: 9 · 2019: 7 · 2018: 4 · 2017: 4 · 2016: 12 · 2015: 13 · 2014: 5 · 2013: 6 · 2012: 1
- FWCI
- 3.21
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- The EMBO Journal (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Keywords
- nuclear pore complex assembly, nuclear envelope, membrane binding, protein dimerization, nucleoporins, membrane deformation, C-terminal domain, interphase, yeast, vertebrates
- MeSH terms
- Amino Acid Sequence, Animals, Binding Sites, HeLa Cells, Humans, Interphase, Liposomes, Membrane Fusion, Molecular Sequence Data, Protein Binding, Structure-Activity Relationship, Xenopus laevis, Mutagenesis, Site-Directed, Conserved Sequence, Protein Structure, Tertiary, Dimerization, Nuclear Pore, Nuclear Pore Complex Proteins, Saccharomyces cerevisiae Proteins, Xenopus Proteins
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