ArticleProceedings of the National Academy of Sciences of the United States of America2013
Ring cycle for dilating and constricting the nuclear pore.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- Tetraspanin-enriched microdomains play an important role in pathogenesis in the protozoan parasite Entamoeba histolytica.PLoS pathogens · 2024Article
- Unveiling the complexity: assessing models describing the structure and function of the nuclear pore complex.Frontiers in cell and developmental biology · 2023Review
- Understanding the role of mechanics in nucleocytoplasmic transport.APL bioengineering · 2022Article
- The yellow brick road to nuclear membrane mechanotransduction.APL bioengineering · 2022Review
- Nuclear lamins: Structure and function in mechanobiology.APL bioengineering · 2022Review
- On the nuclear pore complex and its emerging role in cellular mechanotransduction.APL bioengineering · 2022Review
- Location, location, location: subcellular protein partitioning in proteostasis and aging.Biophysical reviews · 2021Review
- Free energy calculations shed light on the nuclear pore complex's selective barrier nature.Biophysical journal · 2021Article
- Article
- Adapter Proteins for Opposing Motors Interact Simultaneously with Nuclear Pore Protein Nup358.Biochemistry · 2019Article
- 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
- Mechanosensing at the Nuclear Envelope by Nuclear Pore Complex Stretch Activation and Its Effect in Physiology and Pathology.Frontiers in physiology · 2019Article
- Single Cell Imaging of Nuclear Architecture Changes.Frontiers in cell and developmental biology · 2019Article
- A Quantitative Model for BicD2/Cargo Interactions.Biochemistry · 2018Article
- Emerging views of the nucleus as a cellular mechanosensor.Nature cell biology · 2018Review
- Electron microscopy of Chaetomium pom152 shows the assembly of ten-bead string.Cell discovery · 2018Article
- A coarse-grained computational model of the nuclear pore complex predicts Phe-Gly nucleoporin dynamics.The Journal of general physiology · 2017Article
- Protein Transport by the Nuclear Pore Complex: Simple Biophysics of a Complex Biomachine.Biophysical journal · 2017Review
- Nuclear membrane stretch and its role in mechanotransduction.Nucleus (Austin, Tex.) · 2017Review
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3 authors.
Funding
Abstract
We recently showed that the three "channel" nucleoporins, Nup54, Nup58, and Nup62, interact with each other through only four distinct sites and established the crystal structures of the two resulting "interactomes," Nup54•Nup58 and Nup54•Nup62. We also reported instability of the Nup54•Nup58 interactome and previously determined the atomic structure of the relevant Nup58 segment by itself, demonstrating that it forms a twofold symmetric tetramer. Here, we report the crystal structure of the relevant free Nup54 segment and show that it forms a tetrameric, helical bundle that is structurally "conditioned" for instability by a central patch of polar hydrogen-bonded residues. Integrating these data with our previously reported results, we propose a "ring cycle" for dilating and constricting the nuclear pore. In essence, three homooligomeric rings, one consisting of eight modules of Nup58 tetramers, and two, each consisting of eight modules of Nup54 tetramers, are stacked in midplane and characterize a constricted pore of 10- to 20-nm diameter. In going to the dilated state, segments of one Nup58 and two Nup54 tetrameric modules reassort into a dodecameric module, eight of which form a single, heterooligomeric midplane ring, which is flexible in a diameter range of 40-50 nm. The ring cycle would be regulated by phenylalanine-glycine regions ("FG repeats") of channel nups. Akin to ligand-gated channels, the dilated state of the midplane ring may be stabilized by binding of [cargo•transport-factor] complexes to FG repeats, thereby linking the ratio of constricted to dilated nuclear pores to cellular transport need.
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