ArticleThe Journal of biological chemistry2012
Nucleoporin Nup50 stabilizes closed conformation of armadillo repeat 10 in importin α5.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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
20 citing papers in PubMed.
- Breaking barriers: Respiratory viral strategies targeting the host's nuclear pore complex and nuclear transport pathways.Molecular biology of the cell · 2026Review
- Ran modulates allosteric crosstalk between importin β surfaces.Nature communications · 2025Article
- Advances in the understanding of nuclear pore complexes in human diseases.Journal of cancer research and clinical oncology · 2024Review
- Article
- Nup50 plays more than one instrument.Cell cycle (Georgetown, Tex.) · 2022Article
- The Hitchhiker's Guide to Nucleocytoplasmic Trafficking in Neurodegeneration.Neurochemical research · 2020Review
- The Structure of the Nuclear Pore Complex (An Update).Annual review of biochemistry · 2019Review
- Evolutionary divergence of the nuclear pore complex from fungi to metazoans.Protein science : a publication of the Protein Society · 2019Article
- Synergy of two low-affinity NLSs determines the high avidity of influenza A virus nucleoprotein NP for human importin α isoforms.Scientific reports · 2017Article
- Distinctive Properties of the Nuclear Localization Signals of Inner Nuclear Membrane Proteins Heh1 and Heh2.Structure (London, England : 1993) · 2015Article
- Diversification of importin-α isoforms in cellular trafficking and disease states.The Biochemical journal · 2015Review
- Molecular determinants for nuclear import of influenza A PB2 by importin α isoforms 3 and 7.Structure (London, England : 1993) · 2015Article
- Structure of Importin-α from a Filamentous Fungus in Complex with a Classical Nuclear Localization Signal.PloS one · 2015Article
- Compounds with anti-influenza activity: present and future of strategies for the optimal treatment and management of influenza. Part I: Influenza life-cycle and currently available drugs.Journal of preventive medicine and hygiene · 2014Review
- Nup50 is required for cell differentiation and exhibits transcription-dependent dynamics.Molecular biology of the cell · 2014Article
- Design rules for selective binding of nuclear localization signals to minor site of importin α.PloS one · 2014Article
- Exploration of binary virus-host interactions using an infectious protein complementation assay.Molecular & cellular proteomics : MCP · 2013Article
- The Nup153-Nup50 protein interface and its role in nuclear import.The Journal of biological chemistry · 2012Article
- Small terminase couples viral DNA binding to genome-packaging ATPase activity.Structure (London, England : 1993) · 2012Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
The human genome encodes six isoforms of importin α that show greater than 60% sequence similarity and remarkable substrate specificity. The isoform importin α5 can bind phosphorylated cargos such as STAT1 and Epstein-Barr Virus Nuclear Antigen 1, as well as the influenza virus polymerase subunit PB2. In this work, we have studied the interaction of the nucleoporin Nup50 with importin α5. We show that the first 47 residues of Nup50 bind to the C terminus of importin α5 like a "clip," stabilizing the closed conformation of ARM 10. In vitro, Nup50 binds with high affinity either to empty importin α5 or to a preassembled complex of importin α5 bound to the C-terminal domain of the import cargo PB2, resulting in a trimeric complex. By contrast, PB2 can only bind with high affinity to importin α5 in the absence of Nup50. This suggests that Nup50 primary function may not be to actively displace the import cargo from importin α5 but rather to prevent cargo rebinding in preparation for recycling. This is the first evidence for a nucleoporin modulating the import reaction by directly altering the three-dimensional structure of an import adaptor.
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.