ArticleeLife2013
Scaffold nucleoporins Nup188 and Nup192 share structural and functional properties with nuclear transport receptors.
Article in eLife, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed.
- Building peroxisomes: perspectives on plant peroxins.Biochemical Society transactions · 2026Review
- A checkpoint function for Nup98 in nuclear pore formation suggested by novel inhibitory nanobodies.The EMBO journal · 2024Article
- Phosphorylation of the alpha-I motif in SYMRK drives root nodule organogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The role of the FSGS disease gene product and nuclear pore protein NUP205 in regulating nuclear localization and activity of transcriptional regulators YAP and TAZ.Human molecular genetics · 2023Article
- Nuclear Import and Export of YAP and TAZ.Cancers · 2023Review
- Barrier properties of Nup98 FG phases ruled by FG motif identity and inter-FG spacer length.Nature communications · 2023Article
- Structure and Function of the Nuclear Pore Complex.Cold Spring Harbor perspectives in biology · 2022Review
- 8 Å structure of the outer rings of the Xenopus laevis nuclear pore complex obtained by cryo-EM and AI.Protein & cell · 2022Article
- Architecture of the cytoplasmic face of the nuclear pore.Science (New York, N.Y.) · 2022Article
- Architecture of the linker-scaffold in the nuclear pore.Science (New York, N.Y.) · 2022Article
- Near-atomic structure of the inner ring of the Saccharomyces cerevisiae nuclear pore complex.Cell research · 2022Article
- Review
- Cryo-EM structure of the nuclear ring from Xenopus laevis nuclear pore complex.Cell research · 2022Article
- Atomic resolution dynamics of cohesive interactions in phase-separated Nup98 FG domains.Nature communications · 2022Article
- Article
- Article
- Structure of the cytoplasmic ring of the Xenopus laevis nuclear pore complex by cryo-electron microscopy single particle analysis.Cell research · 2020Article
- Differential turnover of Nup188 controls its levels at centrosomes and role in centriole duplication.The Journal of cell biology · 2020Article
- Article
- DNA methylomes and transcriptomes analysis reveal implication of host DNA methylation machinery in BmNPV proliferation in Bombyx mori.BMC genomics · 2019Article
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9 authors.
Funding
Abstract
Nucleocytoplasmic transport is mediated by nuclear pore complexes (NPCs) embedded in the nuclear envelope. About 30 different proteins (nucleoporins, nups) arrange around a central eightfold rotational axis to build the modular NPC. Nup188 and Nup192 are related and evolutionary conserved, large nucleoporins that are part of the NPC scaffold. Here we determine the structure of Nup188. The protein folds into an extended stack of helices where an N-terminal 130 kDa segment forms an intricate closed ring, while the C-terminal region is a more regular, superhelical structure. Overall, the structure has distant similarity with flexible S-shaped nuclear transport receptors (NTRs). Intriguingly, like NTRs, both Nup188 and Nup192 specifically bind FG-repeats and are able to translocate through NPCs by facilitated diffusion. This blurs the existing dogma of a clear distinction between stationary nups and soluble NTRs and suggests an evolutionary relationship between the NPC and the soluble nuclear transport machinery. DOI:http://dx.doi.org/10.7554/eLife.00745.001.
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