ArticleStructure (London, England : 1993)2018
Deciphering the "Fuzzy" Interaction of FG Nucleoporins and Transport Factors Using Small-Angle Neutron Scattering.
Article in Structure (London, England : 1993), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 25 citations in OpenAlex.
- Study of microstructure formation in epoxy based systems using small angle neutron scattering.RSC advances · 2025Article
- Integrative mapping reveals molecular features underlying the mechanism of nucleocytoplasmic transport.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- A survey of the specificity and mechanism of 1,6 hexanediol-induced disruption of nuclear transport.Nucleus (Austin, Tex.) · 2023Article
- Improving the hole picture: towards a consensus on the mechanism of nuclear transport.Biochemical Society transactions · 2023Article
- Article
- Physical modeling of multivalent interactions in the nuclear pore complex.Biophysical journal · 2021Article
- Phase separation in biology and disease-a symposium report.Annals of the New York Academy of Sciences · 2019Article
- Fuzzy Interactions Form and Shape the Histone Transport Complex.Molecular cell · 2019Article
- Interactions of nuclear transport factors and surface-conjugated FG nucleoporins: Insights and limitations.PloS one · 2019Article
- Methods for Physical Characterization of Phase-Separated Bodies and Membrane-less Organelles.Journal of molecular biology · 2018Review
- Probing Differential Binding Mechanisms of Phenylalanine-Glycine-Rich Nucleoporins by Single-Molecule FRET.Methods in enzymology · 2018Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The largely intrinsically disordered phenylalanine-glycine-rich nucleoporins (FG Nups) underline a selectivity mechanism that enables the rapid translocation of transport factors (TFs) through the nuclear pore complexes (NPCs). Conflicting models of NPC transport have assumed that FG Nups undergo different conformational transitions upon interacting with TFs. To selectively characterize conformational changes in FG Nups induced by TFs we performed small-angle neutron scattering (SANS) with contrast matching. Conformational-ensembles derived from SANS data indicated an increase in the overall size of FG Nups is associated with TF interaction. Moreover, the organization of the FG motif in the interacting state is consistent with prior experimental analyses defining that FG motifs undergo conformational restriction upon interacting with TFs. These results provide structural insights into a highly dynamic interaction and illustrate how functional disorder imparts rapid and selective FG Nup-TF interactions.
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