ArticleBiophysical journal2014
Nuclear pore complex protein sequences determine overall copolymer brush structure and function.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Deciphering the intrinsically disordered characteristics of the FG-Nups through the lens of polymer physics.Nucleus (Austin, Tex.) · 2024Review
- Unveiling the complexity: assessing models describing the structure and function of the nuclear pore complex.Frontiers in cell and developmental biology · 2023Review
- Coacervation of poly-electrolytes in the presence of lipid bilayers: mutual alteration of structure and morphology.Chemical science · 2022Article
- Phosphorylation but Not Oligomerization Drives the Accumulation of Tau with Nucleoporin Nup98.International journal of molecular sciences · 2022Article
- Function of the Nuclear Transport Machinery in Maintaining the Distinctive Compositions of the Nucleus and Cytoplasm.International journal of molecular sciences · 2022Review
- Structure and dynamics of nanoconfined water and aqueous solutions.The European physical journal. E, Soft matter · 2021Review
- Characterizing Binding Interactions That Are Essential for Selective Transport through the Nuclear Pore Complex.International journal of molecular sciences · 2021Article
- Free energy calculations shed light on the nuclear pore complex's selective barrier nature.Biophysical journal · 2021Article
- FG nucleoporins feature unique patterns that distinguish them from other IDPs.Biophysical journal · 2021Article
- DNA-Origami NanoTrap for Studying the Selective Barriers Formed by Phenylalanine-Glycine-Rich Nucleoporins.Journal of the American Chemical Society · 2021Article
- Physics of the Nuclear Pore Complex: Theory, Modeling and Experiment.Physics reports · 2021Article
- Theoretical Modeling of Chemical Equilibrium in Weak Polyelectrolyte Layers on Curved Nanosystems.Polymers · 2020Review
- Polymer translocation through a hairy channel mimicking the inner plug of a nuclear pore complex.European biophysics journal : EBJ · 2019Article
- The Role of Cohesiveness in the Permeability of the Spatial Assemblies of FG Nucleoporins.Biophysical journal · 2019Article
- Simulation methods for liquid-liquid phase separation of disordered proteins.Current opinion in chemical engineering · 2019Article
- Enhanced Nucleocytoplasmic Transport due to Competition for Elastic Binding Sites.Biophysical journal · 2018Article
- IDPs in macromolecular complexes: the roles of multivalent interactions in diverse assemblies.Current opinion in structural biology · 2018Review
- Charge Influences Substrate Recognition and Self-Assembly of Hydrophobic FG Sequences.Biophysical journal · 2017Article
- 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
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The transport of cargo across the nuclear membrane is highly selective and accomplished by a poorly understood mechanism involving hundreds of nucleoporins lining the inside of the nuclear pore complex (NPC). Currently, there is no clear picture of the overall structure formed by this collection of proteins within the pore, primarily due to their disordered nature. We perform coarse-grained simulations of both individual nucleoporins and grafted rings of nups mimicking the in vivo geometry of the NPC and supplement this with polymer brush modeling. Our results indicate that different regions or blocks of an individual NPC protein can have distinctly different forms of disorder and that this property appears to be a conserved functional feature. Furthermore, this block structure at the individual protein level is critical to the formation of a unique higher-order polymer brush architecture that can exist in distinct morphologies depending on the effective interaction energy between the phenylalanine glycine (FG) domains of different nups. Because the interactions between FG domains may be modulated by certain forms of transport factors, our results indicate that transitions between brush morphologies could play an important role in regulating transport across the NPC, suggesting novel forms of gated transport across membrane pores with wide biomimetic applicability.
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