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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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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

Nuclear Export of mRNA

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Nuclear Localization Signals and Import01:46

Nuclear Localization Signals and Import

8.1K
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...
8.1K
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...
3.4K
Nuclear Export01:42

Nuclear Export

5.2K
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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Single-Molecule Imaging of Nuclear Transport
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The Structure Inventory of the Nuclear Pore Complex.

Thomas U Schwartz1

  • 1Department of Biology, Massachusetts Institute of Technology, Cambridge, 02139, MA, USA.

Journal of Molecular Biology
|March 27, 2016
PubMed
Summary

The nuclear pore complex (NPC), a large gateway between the nucleus and cytoplasm, is now easier to study. High-resolution structures of its components enable new assembly models for understanding NPC function, evolution, and assembly.

Keywords:
macromolecular complexesnuclear pore complex

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Area of Science:

  • Cell Biology
  • Structural Biology
  • Biochemistry

Background:

  • The nuclear pore complex (NPC) regulates transport between the nucleus and cytoplasm.
  • NPCs are large molecular machines (50-112MDa) composed of ~500-1000 proteins, posing significant structural challenges.
  • Understanding NPC structure is crucial for cell function and disease research.

Purpose of the Study:

  • To review high-resolution structures of NPC building blocks.
  • To highlight the integration of structural data with cryo-electron microscopy for assembly modeling.
  • To establish a structural basis for future NPC research.

Main Methods:

  • Compilation and analysis of existing high-resolution structural data for NPC proteins.
  • Integration of structural data with cryo-electron microscopy (cryo-EM) techniques.
  • Development of structure-based assembly models for the NPC.

Main Results:

  • A comprehensive collection of high-resolution structures for individual NPC proteins is available.
  • Hybrid approaches combining structural data and cryo-EM enable the generation of NPC assembly models.
  • The first structure-based assembly models of the NPC have been generated.

Conclusions:

  • Advances in structural biology provide unprecedented insights into NPC architecture.
  • Structure-based models are essential for detailed analysis of NPC function, evolution, and assembly.
  • Future research on the NPC will heavily rely on these structural insights.