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Related Concept Videos

Nuclear Protein Sorting01:34

Nuclear Protein Sorting

6.6K
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

Regulation of Nuclear Protein Sorting

3.4K
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 Export01:42

Nuclear Export

5.1K
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...
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Nuclear Export of mRNA02:31

Nuclear Export of mRNA

9.0K
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

Nuclear Export of mRNA

5.6K
5.6K
Nuclear Localization Signals and Import01:46

Nuclear Localization Signals and Import

8.0K
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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Related Experiment Video

Updated: Mar 9, 2026

Single-Molecule Imaging of Nuclear Transport
12:13

Single-Molecule Imaging of Nuclear Transport

Published on: June 9, 2010

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The nuclear pore complex: understanding its function through structural insight.

Martin Beck1, Ed Hurt2

  • 1European Molecular Biology Laboratory, Structural and Computational Biology Unit, Meyerhofstrasse 1, Heidelberg D-69117, Germany.

Nature Reviews. Molecular Cell Biology
|December 22, 2016
PubMed
Summary
This summary is machine-generated.

Nuclear pore complexes (NPCs) form channels in the nuclear envelope. New structural insights reveal a network of short linear motifs organizing NPC components, advancing understanding of their diverse functions.

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Related Experiment Videos

Last Updated: Mar 9, 2026

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

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

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Validation of a Mouse Model to Disrupt LINC Complexes in a Cell-specific Manner

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Area of Science:

  • Cell Biology
  • Structural Biology
  • Molecular Biology

Background:

  • Nuclear pore complexes (NPCs) are essential for nucleocytoplasmic transport, regulating gene expression, chromatin organization, and DNA repair.
  • Understanding NPC molecular mechanisms is crucial, but has been limited by a lack of detailed structural information.
  • Mutations in nucleocytoplasmic transport systems are linked to clinical manifestations.

Purpose of the Study:

  • To elucidate the structural organization of the NPC at a pseudo-atomic level.
  • To understand the role of short linear motifs in NPC spatial organization.
  • To provide a foundation for investigating the molecular basis of NPC-related diseases.

Main Methods:

  • Integration of crystallographic and biochemical analyses of nucleoporins (NUPs).
  • Cryo-electron microscopic imaging of the intact NPC in situ.
  • Analysis of short linear motif networks within the NPC structure.

Main Results:

  • A pseudo-atomic view of the NPC central core was achieved.
  • An unexpected network of short linear motifs was identified as a key organizational principle.
  • The study provides unprecedented structural detail of the NPC.

Conclusions:

  • Recent structural breakthroughs have transformed the understanding of NPC organization.
  • The identified motif network is critical for NPC spatial arrangement and function.
  • This structural knowledge is foundational for future functional studies and disease mechanism elucidation.