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Related Concept Videos

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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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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...
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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
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Nuclear Protein Sorting01:34

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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.
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Regulation of Nuclear Protein Sorting01:45

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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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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...
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The Nuclear Transporter Transportin-3 Functions Under Oxidative Stress.

Megan A L Barling1, David R Thomas1, David A Jans1

  • 1Biomedicine Discovery Institute, Monash University, Clayton, VIC 3800, Australia.

Cells
|April 27, 2026
PubMed
Summary

Nuclear transport proteins, Importin-13 (IMP13) and Transportin-3 (TNPO3), maintain function under oxidative stress. They protect the nuclear transport system by preventing mislocalisation of the key molecule Ran.

Keywords:
Fluorescence Recovery After Photobleaching (FRAP)confocal laser scanning microscopy (CLSM)importin-13 (IMP13)nucleocytoplasmic transportoxidative stresstransportin-3 (TNPO3)

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Nuclear transport regulates essential biomolecule movement between the nucleus and cytoplasm, crucial for cellular function.
  • The Importin (IMP) superfamily tightly controls nuclear transport, but it can be disrupted by cellular stress, particularly oxidative stress.
  • Oxidative stress is implicated in diseases like cancer, viral infections, and metabolic disorders.

Purpose of the Study:

  • To investigate the stress resilience of Transportin-3 (TNPO3), the closest homologue to the stress-resistant Importin-13 (IMP13).
  • To determine if TNPO3, like IMP13, retains nuclear transport functionality under stress conditions.

Main Methods:

  • Phylogenetic and structural analysis to identify IMP13 homologues.
  • Subcellular localization studies to assess protein distribution under stress.
  • Fluorescence recovery after photobleaching (FRAP) to evaluate protein shuttling dynamics.
  • Co-immunoprecipitation assays to examine cargo binding capacity.

Main Results:

  • TNPO3 maintained its typical subcellular localization and shuttling ability (FRAP) even under stress.
  • TNPO3 demonstrated cargo binding capacity in the presence of stress, unlike other IMPs.
  • Both IMP13 and TNPO3 protected against the mislocalisation of Ran, a critical component of the nuclear transport system.

Conclusions:

  • TNPO3, similar to IMP13, retains nuclear transport functionality under stress conditions.
  • This stress resilience of TNPO3 and IMP13 offers a protective mechanism for the nuclear transport system.
  • Findings highlight TNPO3 as a potential therapeutic target for stress-related diseases.