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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...

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...

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The nucleus restricts several proteins within and allows others to pass. The restricted proteins possess a nuclear retention sequence or NRS, anchoring them to the nuclear lamins and preventing their transport to the cytosol. The non-restricted proteins, after their synthesis, are transported to their site of action, such as the cytosol or other organelles, with the help of nuclear export signals or NES.
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Related Experiment Video

Updated: May 20, 2026

Assay to Measure Nucleocytoplasmic Transport in Real Time within Motor Neuron-like NSC-34 Cells

Assay to Measure Nucleocytoplasmic Transport in Real Time within Motor Neuron-like NSC-34 Cells

Published on: May 16, 2017

[An efficient high-throughput screening assay against nuclear transport].

Min Luo¹, Quan-Cang Zhang, Zhi-Gang Lu

¹ShenzhenCenter for Disease Control and Prevention, Shenzhen 518055, China. luomin4653@163.net

Yi Chuan = Hereditas

|July 19, 2012

Summary

Researchers developed a novel assay to screen for small molecules regulating nuclear transport. This system uses reconstituted GFP fluorescence to detect changes in nuclear transport, aiding drug discovery for diseases like cancer.

Related Experiment Videos

Last Updated: May 20, 2026

Assay to Measure Nucleocytoplasmic Transport in Real Time within Motor Neuron-like NSC-34 Cells

Assay to Measure Nucleocytoplasmic Transport in Real Time within Motor Neuron-like NSC-34 Cells

Published on: May 16, 2017

Area of Science:

Molecular Biology
Cell Biology
Drug Discovery

Background:

Nuclear transport is crucial for eukaryotic cell function, impacting differentiation, development, viral diseases, and oncogenesis.
Targeting nuclear transport with small molecules is vital for fundamental research and disease treatment.
Currently, Leptomycin B is the sole commercially available inhibitor, highlighting the need for new screening methods.

Purpose of the Study:

To establish an efficient assay for screening small molecules that regulate the entire nuclear transport pathway.
To enable high-throughput screening for novel nuclear transport modulators.
To provide a tool for fundamental research and potential therapeutic development.

Main Methods:

Developed a nuclear transport assay based on the reconstitution of green fluorescent protein (GFP) from two complementary fragments: NZGFP and CZGFP.
Engineered NZGFP with a Nuclear Export Signal (NES) to localize in the cytoplasm and CZGFP with a Nuclear Localization Signal (NLS) to localize in the nucleus.
Utilized the system's sensitivity to detect the inhibitory effect of Leptomycin B on nuclear transport by observing GFP reconstitution upon transport interference.

Main Results:

Successfully established an efficient nuclear transport assay using the NZGFP-NES and CZGFP-NLS reporter system.
Demonstrated that the assay sensitively detects the inhibition of nuclear transport by Leptomycin B.
The system allows for the detection of altered protein localization and subsequent GFP reconstitution when nuclear transport is modulated.

Conclusions:

The developed NZGFP-NES/CZGFP-NLS reporter system provides an efficient method for high-throughput screening of small molecules targeting nuclear transport.
This assay facilitates the discovery of novel compounds that regulate nuclear transport, with potential applications in fundamental research and disease treatment.
The system's sensitivity and efficiency make it a valuable tool for identifying new therapeutic agents.