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Related Concept Videos

Nuclear Protein Sorting01:34

Nuclear Protein Sorting

4.8K
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...
4.8K
Nuclear Export of mRNA02:31

Nuclear Export of mRNA

7.1K
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...
7.1K
Nuclear Export of mRNA02:31

Nuclear Export of mRNA

4.7K
4.7K
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

2.5K
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...
2.5K
Nuclear Export01:42

Nuclear Export

3.7K
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...
3.7K
Nuclear Localization Signals and Import01:46

Nuclear Localization Signals and Import

6.2K
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...
6.2K

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Related Experiment Video

Updated: May 2, 2026

Heterokaryon Technique for Analysis of Cell Type-specific Localization
09:31

Heterokaryon Technique for Analysis of Cell Type-specific Localization

Published on: March 11, 2011

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Cancer and the nuclear pore complex.

Dan N Simon1, Michael P Rout

  • 1The Laboratory of Cellular and Structural Biology, The Rockefeller University, New York, NY, 10065, USA, dsimon01@rockefeller.edu.

Advances in Experimental Medicine and Biology
|February 25, 2014
PubMed
Summary

Nuclear pore complex (NPC) proteins, known as nucleoporins, are increasingly linked to cancer. Mutations and mislocalization of these key trafficking proteins can drive tumorigenesis and viral infection.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Cancer Biology

Background:

  • The nuclear pore complex (NPC) regulates transport between the cytoplasm and nucleoplasm.
  • NPCs are crucial for chromatin silencing, transcriptional regulation, and DNA damage repair.
  • Nucleoporins, NPC structural components, are implicated in various cancers via mutations and altered expression.

Purpose of the Study:

  • To review the roles of nucleoporins in cancer development.
  • To highlight specific nucleoporins associated with tumorigenesis and mRNA export.
  • To explore the connection between viral infections and cancer-associated nucleoporins.

Main Methods:

  • Literature review of studies on nucleoporins and cancer.
  • Analysis of nucleoporin mutations, expression levels, and localization in tumors.

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Single-Molecule Imaging of Nuclear Transport
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Single-Molecule Imaging of Nuclear Transport

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A Direct Force Probe for Measuring Mechanical Integration Between the Nucleus and the Cytoskeleton
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A Direct Force Probe for Measuring Mechanical Integration Between the Nucleus and the Cytoskeleton

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Related Experiment Videos

Last Updated: May 2, 2026

Heterokaryon Technique for Analysis of Cell Type-specific Localization
09:31

Heterokaryon Technique for Analysis of Cell Type-specific Localization

Published on: March 11, 2011

19.0K
Single-Molecule Imaging of Nuclear Transport
12:13

Single-Molecule Imaging of Nuclear Transport

Published on: June 9, 2010

12.7K
A Direct Force Probe for Measuring Mechanical Integration Between the Nucleus and the Cytoskeleton
05:47

A Direct Force Probe for Measuring Mechanical Integration Between the Nucleus and the Cytoskeleton

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  • Examination of viral interactions with cancer-linked nucleoporins.

    • Main Results:

    • Several nucleoporins (Nup62, Nup88, Nup98, Nup214, Nup358/RanBP2, Tpr) are linked to cancer, particularly through mRNA export pathways.
    • Oncogenic nucleoporin mutants exhibit mislocalization or altered NPC incorporation, disrupting signaling and transcription.
    • Viruses frequently target these same cancer-associated nucleoporins, suggesting exploitation of cellular vulnerabilities.

    Conclusions:

    • Nucleoporins play significant roles in cancer pathogenesis.
    • Dysregulation of nucleoporins contributes to altered cellular functions and disease.
    • Targeting cancer-associated nucleoporins presents potential therapeutic avenues and insights into viral pathogenesis.