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Related Concept Videos

Regulation of Nuclear Protein Sorting01:45

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 Sorting01:34

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 Export01:42

Nuclear Export

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.
NES are of three types- the canonical 10-residue long leucine-rich signal and other...
Nuclear Localization Signals and Import01:46

Nuclear Localization Signals and Import

Proteins targeted to the nucleus carry short stretches of amino acid sequences called the nuclear localization signal or NLS. Classical nuclear localization signals are of two types: monopartite and bipartite NLS. Monopartite classical NLS (cNLS) consists of a single cluster of 4-8 amino acids. Bipartite cNLS consists of two clusters of  2-3 amino acids and a 9-12 residue long proline-rich linker bridging the two clusters. Signal clusters are rich in positively charged amino acids such as...
Directionality of Nuclear Transport01:42

Directionality of Nuclear Transport

Ras-related nuclear protein or Ran is a small G protein that cycles between its GTP and GDP bound states. Ran specific regulators, a Ran GTPase Activating Protein or RanGAP present in the cytosol and a Ran guanine nucleotide exchange factor or RanGEF present inside the nucleus regulate GTP/GDP exchange. A high concentration of GTP inside the cells, in addition to this asymmetric distribution of  Ran-specific regulators, leads to a higher RanGTP concentration inside the nucleus. This...
Nuclear Export of mRNA02:31

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...

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Related Experiment Video

Updated: May 11, 2026

Single-Molecule Imaging of Nuclear Transport
12:13

Single-Molecule Imaging of Nuclear Transport

Published on: June 9, 2010

Intermolecular disulfide bonds between nucleoporins regulate karyopherin-dependent nuclear transport.

Shige H Yoshimura1, Shotaro Otsuka, Masahiro Kumeta

  • 1Graduate School of Biostudies, Kyoto University, Yoshida-konoe-cho, Sakyo-ku, Kyoto 606-8501, Japan. yoshimura@lif.kyoto-u.ac.jp

Journal of Cell Science
|May 4, 2013
PubMed
Summary

Disulfide bonds in nucleoporins (Nups) regulate nuclear transport. Oxidative stress induces Nup S-S bond formation, altering nuclear pore complex (NPC) permeability.

Keywords:
Disulfide bridgeImportin βNuclear poreNucleocytoplasmic transportOxidative stress

Related Experiment Videos

Last Updated: May 11, 2026

Single-Molecule Imaging of Nuclear Transport
12:13

Single-Molecule Imaging of Nuclear Transport

Published on: June 9, 2010

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Disulfide (S-S) bonds are crucial for protein function and cellular stress responses.
  • Nucleoporins (Nups) form the nuclear pore complex (NPC), regulating transport between the nucleus and cytoplasm.

Purpose of the Study:

  • To investigate the role of Nup S-S bond formation in regulating nuclear transport.
  • To determine how intracellular redox state affects NPC permeability.

Main Methods:

  • Kinetic analysis of importin β transport.
  • Treatment with reducing (dithiothreitol) and oxidative agents.
  • Immunoblot analysis of Nups.
  • Site-directed mutagenesis of cysteine residues in Nup62.
  • Nup62 knockdown experiments.

Main Results:

  • NPC permeability increased with dithiothreitol and decreased with oxidative stress.
  • Oxidative stress induced S-S bond formation in Nup358, Nup155, Nup153, and Nup62.
  • Mutating cysteine residues in Nup62 abolished S-S bond formation and increased NPC permeability.
  • Nup62 knockdown reduced stress-induced S-S bonds in Nup155, indicating a covalent link.

Conclusions:

  • Nups form S-S bonds that modulate NPC permeability and nuclear transport.
  • The NPC's inner channel is sensitive to intracellular redox state, suggesting compartmentalization of redox environments.