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Regulation of Nuclear Protein Sorting

Regulation of Nuclear Protein Sorting

Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...

Nuclear Protein Sorting

Nuclear Protein Sorting

Nuclear protein sorting is the selective trafficking of histones, polymerases, gene regulatory proteins into the nucleus and exporting RNAs and ribosomes to the cytosol. It is a tightly controlled process that regulates gene expression within a cell.
Proteins targeted to the nucleus carry nuclear localization signals or NLS recognized by import receptors in the cytosol. Similarly, proteins with nuclear export signals are recognized by export receptors. Import and export receptors are...

Nuclear Export of mRNA

Nuclear Export of mRNA

Before mRNAs are exported to the cytoplasm, it is crucial to check each mRNA for structural and functional integrity. Eukaryotic cells use several different mechanisms, collectively known as mRNA surveillance, to look for irregularities in mRNAs. Irregular or aberrant mRNA are rapidly degraded by various enzymes. If a defective mRNA escapes the surveillance, it would be translated into a protein which would either be non-functional or not function properly. One of the primary irregularities in...

Nuclear Export of mRNA

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Before mRNAs are exported to the cytoplasm, it is crucial to check each mRNA for structural and functional integrity. Eukaryotic cells use several different mechanisms, collectively known as mRNA surveillance, to look for irregularities in mRNAs. Irregular or aberrant mRNA are rapidly degraded by various enzymes. If a defective mRNA escapes the surveillance, it would be translated into a protein which would either be non-functional or not function properly. One of the primary irregularities in...

Nuclear Export

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Membrane Asymmetry Regulating Transporters

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Flippase
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Related Experiment Video

Updated: May 22, 2026

Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution

Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution

Published on: August 16, 2016

Self-regulated viscous channel in the nuclear pore complex.

Jiong Ma¹, Alexander Goryaynov, Ashapurna Sarma

¹Department of Biological Sciences, Center for Photochemical Sciences, Bowling Green State University, Bowling Green, OH 43403, USA.

Proceedings of the National Academy of Sciences of the United States of America

|April 25, 2012

Summary

The nuclear pore complex has a single viscous channel for small molecule diffusion. Transport receptors use distinct peripheral routes, revealing a self-regulated channel model over a porous network.

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Single-Molecule Imaging of Nuclear Transport

Single-Molecule Imaging of Nuclear Transport

Published on: June 9, 2010

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Last Updated: May 22, 2026

Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution

Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution

Published on: August 16, 2016

Single-Molecule Imaging of Nuclear Transport

Single-Molecule Imaging of Nuclear Transport

Published on: June 9, 2010

Area of Science:

Cell Biology
Molecular Biology
Biophysics

Background:

The nuclear pore complex (NPC) regulates transport between the nucleus and cytoplasm.
Models debate whether small molecules diffuse through a single channel or a porous hydrogel network within the NPC.
The spatial relationship between passive and facilitated transport pathways in the NPC is unclear.

Purpose of the Study:

To investigate the physical pathways for passive and facilitated transport through the human NPC.
To differentiate between the viscous channel and hydrogel meshwork models of NPC transport.
To determine if transport pathways are spatially segregated or overlapping.

Main Methods:

Utilized three-dimensional super-resolution fluorescence microscopy in human cells.
Visualized the structure and dynamics of the NPC during nucleocytoplasmic transport.
Applied advanced imaging techniques to track small molecules and transport complexes.

Main Results:

Demonstrated that a single viscous central channel serves as the exclusive pathway for passive diffusion of small molecules.
Identified distinct peripheral routes for transport receptors and cargo, occluded by phenylalanine-glycine filaments.
Showed that passive and facilitated transport pathways are correlated and co-regulated by Importin β1 and RanGTP.

Conclusions:

The findings strongly support a self-regulated viscous channel model for native NPCs.
The results refute the porous hydrogel meshwork model for NPC passive diffusion.
NPC transport pathways are spatially organized and dynamically regulated by key transport factors.