A coarse-grained computational model of the nuclear pore complex predicts Phe-Gly nucleoporin dynamics

  title={A coarse-grained computational model of the nuclear pore complex predicts Phe-Gly nucleoporin dynamics},
  author={Joan Pulupa and Manas Rachh and Michael D. Tomasini and Joshua S. Mincer and Sanford M. Simon},
  journal={The Journal of General Physiology},
  pages={951 - 966}
The phenylalanine-glycine–repeat nucleoporins (FG-Nups), which occupy the lumen of the nuclear pore complex (NPC), are critical for transport between the nucleus and cytosol. Although NPCs differ in composition across species, they are largely conserved in organization and function. Transport through the pore is on the millisecond timescale. Here, to explore the dynamics of nucleoporins on this timescale, we use coarse-grained computational simulations. These simulations generate predictions… 
4 Citations

Figures from this paper

Modeling the nucleoporins that form the hairy pores.
Different methods employed in modeling the FG-Nups are reviewed, arranging from all-atom molecular dynamics to mean-field theories, and the advantage and limit of each modeling technique are discussed, and theoretical insights that are summarized deepened the understanding of the hairy pore are summarized.
On the nuclear pore complex and its emerging role in cellular mechanotransduction
The nuclear pore complex is a large protein assembly that perforates the nuclear envelope and provides a sole gateway for traffic between the cytoplasm and the nucleus, playing a vital role in protecting the nuclear component and regulating gene expression and protein synthesis.
Super-resolved 3D tracking of cargo transport through nuclear pore complexes
A multicolour imaging approach is reported that enables direct three-dimensional visualization of cargo transport trajectories relative to a super-resolved octagonal double-ring structure of the NPC scaffold in non-fixed permeabilized cells.


Brownian Dynamics Simulation of Nucleocytoplasmic Transport: A Coarse-Grained Model for the Functional State of the Nuclear Pore Complex
This work has established a coarse-grained model of the NPC structure that mimics nucleocytoplasmic transport and shows a high degree of permeability to inert cargos, implying the defining role of cytoplasmsic filaments in the selectivity barrier.
Assembly of Nsp1 Nucleoporins Provides Insight into Nuclear Pore Complex Gating
The authors' simulations suggest that the NPC central channel features brush-like moderately cross-linked bundles, but in the central region, where tethering loses its effect, features a sieve-like structure of bundles and frequent cross-links.
Nucleoporin's Like Charge Regions Are Major Regulators of FG Coverage and Dynamics Inside the Nuclear Pore Complex
This study further explores the role of LCRs in the distribution of FG Nups, using a recently developed coarse-grained molecular dynamics model and demonstrates how L CRs affect the formation of two transport pathways.
Simple biophysics underpins collective conformations of the intrinsically disordered proteins of the Nuclear Pore Complex
It is shown that the spatial organization of FG nucleoporin assemblies with the transport proteins can be understood within a first principles biophysical model with a minimal number of key physical variables, such as the average protein interaction strengths and spatial densities.