ArticleProceedings of the National Academy of Sciences of the United States of America2008
Individual binding pockets of importin-beta for FG-nucleoporins have different binding properties and different sensitivities to RanGTP.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. 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, 65 citations in OpenAlex.
- Ran modulates allosteric crosstalk between importin β surfaces.Nature communications · 2025Article
- Charge of karyopherins and nuclear FG-Nups are key ingredients of nucleocytoplasmic transport.Biophysical journal · 2025Article
- Article
- Interaction modules that impart specificity to disordered protein.Trends in biochemical sciences · 2023Review
- Nuclear import receptors are recruited by FG-nucleoporins to rescue hallmarks of TDP-43 proteinopathy.Molecular neurodegeneration · 2022Article
- Crosstalk between nucleocytoplasmic trafficking and the innate immune response to viral infection.The Journal of biological chemistry · 2021Review
- Nucleoplasmic signals promote directed transmembrane protein import simultaneously via multiple channels of nuclear pores.Nature communications · 2020Article
- Article
- Floppy but not sloppy: Interaction mechanism of FG-nucleoporins and nuclear transport receptors.Seminars in cell & developmental biology · 2017Review
- In vivo analysis of protein crowding within the nuclear pore complex in interphase and mitosis.Scientific reports · 2017Article
- Importin β1 targeting by hepatitis C virus NS3/4A protein restricts IRF3 and NF-κB signaling of IFNB1 antiviral response.Traffic (Copenhagen, Denmark) · 2017Article
- The selective permeability barrier in the nuclear pore complex.Nucleus (Austin, Tex.) · 2016Review
- The Multiple Faces of Disordered Nucleoporins.Journal of molecular biology · 2016Review
- Article
- Plasticity of an ultrafast interaction between nucleoporins and nuclear transport receptors.Cell · 2015Article
- MD simulations and FRET reveal an environment-sensitive conformational plasticity of importin-β.Biophysical journal · 2015Article
- Role of molecular charge in nucleocytoplasmic transport.PloS one · 2014Article
- Single-molecule analysis of the recognition forces underlying nucleo-cytoplasmic transport.Angewandte Chemie (International ed. in English) · 2013Article
- Epstein-Barr virus protein kinase BGLF4 targets the nucleus through interaction with nucleoporins.Journal of virology · 2012Article
- Self-regulated viscous channel in the nuclear pore complex.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
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 at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Importin-beta mediates protein transport across the nuclear envelope through the nuclear pore complex (NPC) by interacting with components of the NPC, called nucleoporins, and a small G protein, Ran. Although there is accumulated knowledge on the specific interaction between importin-beta and the Phe-Gly (FG) motif in the nucleoporins as well as the effect of RanGTP on this interaction, the molecular mechanism by which importin-beta shuttles across the nuclear envelope through the NPC is unknown. In this study, we focused on four binding pockets of importin-beta for the FG motifs and characterized the interaction using a single-molecule force-measurement technique with atomic-force microscopy. The results from a series of importin-beta mutants containing amino acid substitutions within the FG-binding pockets demonstrate that the individual FG-binding pockets have different affinities to FG-Nups (Nup62 and Nup153) and different sensitivities to RanGTP; the binding of RanGTP to the amino-terminal domain of importin-beta induces the conformational change of the entire molecule and reduces the affinity of some of the pockets but not others. These heterogeneous characteristics of the multiple FG-binding pockets may play an important role in the behavior of importin-beta within the NPC. Single-molecule force measurement using the entire molecule of an NPC from a Xenopus oocyte also implies that the reduction of the affinity by RanGTP really occurs at the nucleoplasmic side of the entire NPC.
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.