ArticleMolecular biology of the cell2014
The stoichiometry of the nucleoporin 62 subcomplex of the nuclear pore in solution.
Article in Molecular biology of the cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 28 citations in OpenAlex.
- Interactions between FUS and the C-terminal Domain of Nup62 are Sufficient for their Co-phase Separation into Amorphous Assemblies.Journal of molecular biology · 2023Article
- Insights into the role of Nup62 and Nup93 in assembling cytoplasmic ring and central transport channel of the nuclear pore complex.Molecular biology of the cell · 2022Article
- Co-translational assembly orchestrates competing biogenesis pathways.Nature communications · 2022Article
- Article
- Molecular and structural analysis of central transport channel in complex with Nup93 of nuclear pore complex.Protein science : a publication of the Protein Society · 2020Article
- The Structure of the Nuclear Pore Complex (An Update).Annual review of biochemistry · 2019Review
- Exploitation of reverse vaccinology and immunoinformatics as promising platform for genome-wide screening of new effective vaccine candidates against Plasmodium falciparum.BMC bioinformatics · 2019Article
- Nucleoporin Nup58 localizes to centrosomes and mid-bodies during mitosis.Cell division · 2019Article
- The nuclear pore complex: understanding its function through structural insight.Nature reviews. Molecular cell biology · 2017Review
- Systematic Protein-Protein Interaction Analysis Reveals Intersubcomplex Contacts in the Nuclear Pore Complex.Molecular & cellular proteomics : MCP · 2016Article
- Review
- 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
- Analysis of the initiation of nuclear pore assembly by ectopically targeting nucleoporins to chromatin.Nucleus (Austin, Tex.) · 2015Article
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
Abstract
The nuclear pore complex (NPC) regulates transport between the nucleus and cytoplasm. Soluble cargo-protein complexes navigate through the pore by binding to phenylalanine-glycine (FG)-repeat proteins attached to the channel walls. The Nup62 complex contains the FG-repeat proteins Nup62, Nup54, and Nup58 and is located in the center of the NPC. The three proteins bind each other via conserved coiled-coil segments. To determine the stoichiometry of the Nup62 complex, we undertook an in vitro study using gel filtration and analytical ultracentrifugation. Our results reveal a 1:1:1 stoichiometry of the Nup62 complex, where Nup54 is central with direct binding to Nup62 and Nup58. At high protein concentration, the complex forms larger assemblies while maintaining the Nup62:Nup54:Nup58 ratio. For the homologous Nsp1 complex from Saccharomyces cerevisiae, we determine the same stoichiometry, indicating evolutionary conservation. Furthermore, we observe that eliminating one binding partner can result in the formation of complexes with noncanonical stoichiometry, presumably because unpaired coiled-coil elements tend to find a promiscuous binding partner. We suggest that these noncanonical stoichiometries observed in vitro are unlikely to be physiologically relevant.
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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.