ArticleProceedings of the National Academy of Sciences of the United States of America2014
Evidence for an evolutionary relationship between the large adaptor nucleoporin Nup192 and karyopherins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026Review
- Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025Review
- Identifying and characterizing a missing peroxin-PEX8-in Arabidopsis thaliana.The Plant cell · 2025Article
- Evolutionary trajectory for nuclear functions of ciliary transport complex proteins.Microbiology and molecular biology reviews : MMBR · 2024Review
- Nuclear transport proteins: structure, function, and disease relevance.Signal transduction and targeted therapy · 2023Review
- 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 linker-scaffold in the nuclear pore.Science (New York, N.Y.) · 2022Article
- Architecture of the cytoplasmic face of the nuclear pore.Science (New York, N.Y.) · 2022Article
- Review
- Co-translational assembly orchestrates competing biogenesis pathways.Nature communications · 2022Article
- 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
- The Quest for the Blueprint of the Nuclear Pore Complex.The protein journal · 2019Review
- The Structure of the Nuclear Pore Complex (An Update).Annual review of biochemistry · 2019Review
- Fuzzy Interactions Form and Shape the Histone Transport Complex.Molecular cell · 2019Article
- Pore timing: the evolutionary origins of the nucleus and nuclear pore complex.F1000Research · 2019Review
- Identification of the NovelG3 (Bethesda, Md.) · 2018Article
- Article
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5 authors.
Funding
Abstract
Nucleocytoplasmic transport is facilitated by nuclear pore complexes (NPCs), which are massive proteinaceous transport channels embedded in the nuclear envelope. Nup192 is a major component of an adaptor nucleoporin subcomplex proposed to link the NPC coat with the central transport channel. Here, we present the structure of the ∼110-kDa N-terminal domain (NTD) of Nup192 at 2.7-Å resolution. The structure reveals an open ring-shaped architecture composed of Huntingtin, EF3, PP2A, and TOR1 (HEAT) and Armadillo (ARM) repeats. A comparison of different conformations indicates that the NTD consists of two rigid halves connected by a flexible hinge. Unexpectedly, the two halves of the ring are structurally related to karyopherin-α (Kap-α) and β-karyopherin family members. Biochemically, we identify a conserved patch that binds an unstructured segment in Nup53 and show that a C-terminal tail region binds to a putative helical fragment in Nic96. The Nup53 segment that binds Nup192 is a classical nuclear localization-like sequence that interacts with Kap-α in a mutually exclusive and mechanistically distinct manner. The disruption of the Nup53 and Nic96 binding sites in vivo yields growth and mRNA export defects, revealing their critical role in proper NPC function. Surprisingly, both interactions are dispensable for NPC localization, suggesting that Nup192 possesses another nucleoporin interaction partner. These data indicate that the structured domains in the adaptor nucleoporin complex are held together by peptide interactions that resemble those found in karyopherin•cargo complexes and support the proposal that the adaptor nucleoporins arose from ancestral karyopherins.
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