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Related Concept Videos

Nuclear Protein Sorting01:34

Nuclear Protein Sorting

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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.
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...
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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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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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Eukaryotic cells have different membrane-bound organelles with distinct protein requirements. The process by which proteins are targeted to a specific organelle is called protein sorting.
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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: Mar 7, 2026

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

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SUMO and Nucleocytoplasmic Transport.

Christopher Ptak1, Richard W Wozniak2

  • 1Department of Cell Biology, University of Alberta, Edmonton, AB, T6G 2H7, Canada.

Advances in Experimental Medicine and Biology
|February 16, 2017
PubMed
Summary
This summary is machine-generated.

Nucleocytoplasmic transport and SUMOylation pathways are intricately linked. This review discusses how SUMOylation affects nuclear transport and how transport machinery regulates SUMOylation dynamics.

Keywords:
Nuclear pore complexNucleocytoplasmic transportSUMO

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Last Updated: Mar 7, 2026

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

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Nucleocytoplasmic transport is essential for cellular function, mediating protein exchange between the nucleus and cytoplasm via nuclear pore complexes.
  • Post-translational modifications, such as SUMOylation, play crucial roles in regulating cellular processes, including protein transport.
  • The dynamic interplay between protein transport and modification pathways is critical for maintaining cellular homeostasis.

Purpose of the Study:

  • To review the complex relationship between nucleocytoplasmic transport and SUMO-dependent pathways.
  • To elucidate how SUMOylation influences the nuclear transport machinery and its cargo.
  • To explore how the nuclear transport system regulates SUMOylation and desumoylation processes.

Main Methods:

  • Literature review and synthesis of existing research on nucleocytoplasmic transport and SUMOylation.
  • Analysis of documented examples of SUMOylation affecting nuclear transport.
  • Examination of how nuclear transport machinery impacts SUMOylation dynamics.

Main Results:

  • SUMOylation can inhibit or stimulate nucleocytoplasmic transport by altering cargo properties or directly affecting transport factors.
  • The nuclear transport machinery regulates the localization of SUMOylation/desumoylation enzymes, thereby influencing the sumoylation state of target proteins.
  • Reciprocal regulation exists where transport controls modification, and modification controls transport.

Conclusions:

  • The intricate crosstalk between SUMOylation and nucleocytoplasmic transport is multifaceted, impacting protein localization and cellular function.
  • Understanding these inter-relationships is crucial for comprehending cellular regulation and disease mechanisms.
  • Further research into this interplay can reveal novel therapeutic targets.