Nucleoporins’ exclusive amino acid sequence features regulate their transient interaction with and selectivity of cargo complexes in the nuclear pore-Reference-Cited by-同舟云学术

Nucleoporins’ exclusive amino acid sequence features regulate their transient interaction with and selectivity of cargo complexes in the nuclear pore

Published:2021-11-01 Issue:21 Volume:32 Page:
ISSN:1059-1524
Container-title:Molecular Biology of the Cell
language:en
Short-container-title:MBoC

Author:

Peyro Mohaddeseh¹,Dickson Andrew M.¹,Mofrad Mohammad R. K.¹²

Affiliation:

1. Molecular Cell Biomechanics Laboratory, Departments of Bioengineering and Mechanical Engineering, University of California, Berkeley, CA 94720

2. Molecular Biophysics and Integrative Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720

Abstract

This study integrates coarse-grained molecular dynamics with time-resolved force distribution analysis and bioinformatics inquiry to explore the behavior of disordered proteins FG nucleoporins and their transient interaction with the cargo complex in the nuclear pore.

Publisher

American Society for Cell Biology (ASCB)

Subject

Cell Biology,Molecular Biology

Reference46 articles.

1. The molecular architecture of the nuclear pore complex

2. Physical Motif Clustering within Intrinsically Disordered Nucleoporin Sequences Reveals Universal Functional Features

3. Floppy but not sloppy: Interaction mechanism of FG-nucleoporins and nuclear transport receptors

4. Higher Nucleoporin-Importinβ Affinity at the Nuclear Basket Increases Nucleocytoplasmic Import

5. An agent-based model for mRNA export through the nuclear pore complex

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