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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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Nuclear Export of mRNA02:31

Nuclear Export of mRNA

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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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Nuclear Export of mRNA02:31

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Additional Subnuclear Structures02:10

Additional Subnuclear Structures

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The eukaryotic nucleus is a double membrane-bound organelle that contains nearly all of the cell’s genetic material in the form of chromosomes. It is rightly called the “brain” of the cell as it shoulders the responsibility of responding to various physiological processes, stress, altered metabolic conditions, and other cellular signals. 
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Protein Complex Assembly02:41

Protein Complex Assembly

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Related Experiment Video

Updated: Jan 18, 2026

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

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Structure, function and assembly of nuclear pore complexes.

Stefan Petrovic1,2, George W Mobbs1, André Hoelz3,4

  • 1Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA, USA.

Nature Reviews. Molecular Cell Biology
|September 9, 2025
PubMed
Summary
This summary is machine-generated.

The nuclear pore complex (NPC) regulates molecule transport between the nucleus and cytoplasm in eukaryotic cells. Recent structural studies reveal insights into its function, permeability, and transport mechanisms.

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Related Experiment Videos

Last Updated: Jan 18, 2026

Single-Molecule Imaging of Nuclear Transport
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Published on: June 9, 2010

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Validation of a Mouse Model to Disrupt LINC Complexes in a Cell-specific Manner
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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Structural Biology

Background:

  • Eukaryotic cells compartmentalize genetic material within a nucleus.
  • Efficient transport of macromolecules between the nucleus and cytoplasm is essential for cellular function.
  • The nuclear pore complex (NPC) is a large, conserved protein assembly facilitating regulated nucleocytoplasmic transport.

Purpose of the Study:

  • To review recent advances in understanding nuclear pore complex (NPC) structure and function.
  • To highlight insights gained from near-atomic composite structures of the NPC.
  • To outline future research directions in NPC biology.

Main Methods:

  • Review of recent near-atomic composite structures of the NPC.
  • Analysis of structural data to understand NPC function.
  • Synthesis of current knowledge on nucleocytoplasmic transport.

Main Results:

  • Near-atomic structures provide detailed insights into NPC architecture and function.
  • Advances in understanding the NPC's permeability barrier and transport modes.
  • Identification of key mobile transport factors involved in nucleocytoplasmic exchange.

Conclusions:

  • Recent structural studies have significantly advanced our understanding of the NPC.
  • Further research is needed to elucidate NPC's nuclear basket, mRNA export, biogenesis, and mechanosensation.
  • The NPC remains a critical focus for understanding fundamental eukaryotic cell biology.