ArticleMolecular and cellular biology2001
The Nsp1p carboxy-terminal domain is organized into functionally distinct coiled-coil regions required for assembly of nucleoporin subcomplexes and nucleocytoplasmic transport.
Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
32 citing papers in PubMed.
- Hydrophobic interactions of FG-nucleoporins are required for dilating nuclear membrane pores into selective transport channels after mitosis.Nature structural & molecular biology · 2026Article
- Overexpressed Nup88 stabilized through interaction with Nup62 promotes NF-κB dependent pathways in cancer.Frontiers in oncology · 2023Article
- Acetylation of Nup62 by TIP60 ensures accurate chromosome segregation in mitosis.Journal of molecular cell biology · 2022Article
- Structure of cytoplasmic ring of nuclear pore complex by integrative cryo-EM and AlphaFold.Science (New York, N.Y.) · 2022Article
- Co-translational assembly orchestrates competing biogenesis pathways.Nature communications · 2022Article
- Structure of the cytoplasmic ring of the Xenopus laevis nuclear pore complex by cryo-electron microscopy single particle analysis.Cell research · 2020Article
- The Structure of the Nuclear Pore Complex (An Update).Annual review of biochemistry · 2019Review
- The path of pre-ribosomes through the nuclear pore complex revealed by electron tomography.Nature communications · 2019Article
- Nuclear Pore Complex Components in the Malaria Parasite Plasmodium berghei.Scientific reports · 2018Article
- A Programmable DNA Origami Platform for Organizing Intrinsically Disordered Nucleoporins within Nanopore Confinement.ACS nano · 2018Article
- Architecture of the fungal nuclear pore inner ring complex.Science (New York, N.Y.) · 2015Article
- Linker Nups connect the nuclear pore complex inner ring with the outer ring and transport channel.Nature structural & molecular biology · 2015Article
- Ordered Regions of Channel Nucleoporins Nup62, Nup54, and Nup58 Form Dynamic Complexes in Solution.The Journal of biological chemistry · 2015Article
- Nucleoporin 62-like protein activates canonical Wnt signaling through facilitating the nuclear import of β-catenin in zebrafish.Molecular and cellular biology · 2015Article
- Structural basis for assembly and function of the Nup82 complex in the nuclear pore scaffold.The Journal of cell biology · 2015Article
- Probing the disordered domain of the nuclear pore complex through coarse-grained molecular dynamics simulations.Biophysical journal · 2014Article
- The stoichiometry of the nucleoporin 62 subcomplex of the nuclear pore in solution.Molecular biology of the cell · 2014Article
- Nucleoporin Nup62 maintains centrosome homeostasis.Cell cycle (Georgetown, Tex.) · 2013Article
- Inheritance of yeast nuclear pore complexes requires the Nsp1p subcomplex.The Journal of cell biology · 2013Article
- The transmission of nuclear pore complexes to daughter cells requires a cytoplasmic pool of Nsp1.The Journal of cell biology · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nucleoporin Nsp1p, which has four predicted coiled-coil regions (coils 1 to 4) in the essential carboxy-terminal domain, is unique in that it is part of two distinct nuclear pore complex (NPC) subcomplexes, Nsp1p-Nup57p-Nup49p-Nic96p and Nsp1p-Nup82p-Nup159p. As shown by in vitro reconstitution, coiled-coil region 2 (residues 673 to 738) is sufficient to form heterotrimeric core complexes and can bind either Nup57p or Nup82p. Accordingly, interaction of Nup82p with Nsp1p coil 2 is competed by excess Nup57p. Strikingly, coil 3 and 4 mutants are still assembled into the core Nsp1p-Nup57p-Nup49p complex but no longer associate with Nic96p. Consistently, the Nsp1p-Nup57p-Nup49p core complex dissociates from the nuclear pores in nsp1 coil 3 and 4 mutant cells, and as a consequence, defects in nuclear protein import are observed. Finally, the nsp1-L640S temperature-sensitive mutation, which maps in coil 1, leads to a strong nuclear mRNA export defect. Thus, distinct coiled-coil regions within Nsp1p-C have separate functions that are related to the assembly of different NPC subcomplexes, nucleocytoplasmic transport, and incorporation into the nuclear pores.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.