ArticleThe Journal of biological chemistry2010
The importin beta binding domain modulates the avidity of importin beta for the nuclear pore complex.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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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.
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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.
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Who cites it
29 citing papers in PubMed, 41 citations in OpenAlex.
- NCBP1 promotes the malignant progression of Wilms' tumor through stabilization of KPNA2 mRNA.Cancer gene therapy · 2026Article
- Ran modulates allosteric crosstalk between importin β surfaces.Nature communications · 2025Article
- Yeast 26S proteasome nuclear import is coupled to nucleus-specific degradation of the karyopherin adaptor protein Sts1.Scientific reports · 2024Article
- Structural basis for nuclear import of hepatitis B virus (HBV) nucleocapsid core.Science advances · 2024Article
- Conservation of Importin α Function in Apicomplexans: Ivermectin and GW5074 TargetInternational journal of molecular sciences · 2022Article
- Invasion and Propagation of White Spot Syndrome Virus: Hijacking of the Cytoskeleton, Intracellular Transport Machinery, and Nuclear Import Transporters.Journal of virology · 2022Article
- Nucleoporin 85 interacts with influenza A virus PB1 and PB2 to promote its replication by facilitating nuclear import of ribonucleoprotein.Frontiers in microbiology · 2022Article
- Ubiquitin Ligase Redundancy and Nuclear-Cytoplasmic Localization in Yeast Protein Quality Control.Biomolecules · 2021Review
- Cytoplasmic Parvovirus Capsids Recruit Importin Beta for Nuclear Delivery.Journal of virology · 2020Article
- Review
- Synergy of two low-affinity NLSs determines the high avidity of influenza A virus nucleoprotein NP for human importin α isoforms.Scientific reports · 2017Article
- The Structural Biology of Hepatitis B Virus: Form and Function.Annual review of virology · 2016Review
- Divergent Evolution of Nuclear Localization Signal Sequences in Herpesvirus Terminase Subunits.The Journal of biological chemistry · 2016Article
- Forces, fluctuations, and self-organization in the nucleus.Molecular biology of the cell · 2015Article
- Architecture of the Complex Formed by Large and Small Terminase Subunits from Bacteriophage P22.Journal of molecular biology · 2015Article
- Conservation of inner nuclear membrane targeting sequences in mammalian Pom121 and yeast Heh2 membrane proteins.Molecular biology of the cell · 2015Article
- Distinctive Properties of the Nuclear Localization Signals of Inner Nuclear Membrane Proteins Heh1 and Heh2.Structure (London, England : 1993) · 2015Article
- Molecular determinants for nuclear import of influenza A PB2 by importin α isoforms 3 and 7.Structure (London, England : 1993) · 2015Article
- How to operate a nuclear pore complex by Kap-centric control.Nucleus (Austin, Tex.) · 2015Review
- Disordered proteinaceous machines.Chemical reviews · 2014Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Importin beta mediates active passage of cellular substrates through the nuclear pore complex (NPC). Adaptors such as importin alpha and snurportin associate with importin beta via an importin beta binding (IBB) domain. The intrinsic structural flexibility of importin beta allows its concerted interactions with IBB domains, phenylalanine-glycine nucleoporins, and the GTPase Ran during transport. In this paper, we provide evidence that the nature of the IBB domain modulates the affinity of the import complex for the NPC. In permeabilized cells, importin beta imports a cargo fused to the snurportin IBB (sIBB) with approximately 70% reduced energy requirement as compared with the classical importin alpha IBB. At the molecular level, this is explained by approximately 200-fold reduced affinity of importin beta for Nup62, when bound to the sIBB. Consistently, in vivo, the importin beta.sIBB complex has greatly reduced persistence inside the central channel of the NPC. We propose that by controlling the degree of strain in the tertiary structure of importin beta, the IBB domain modulates the affinity of the import complex for nucleoporins, thus dictating its persistence inside the NPC.
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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.