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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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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 Export01:42

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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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Nuclear Localization Signals and Import01:46

Nuclear Localization Signals and Import

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

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Simple rules for passive diffusion through the nuclear pore complex.

Benjamin L Timney1, Barak Raveh2, Roxana Mironska1

  • 1Laboratory of Cellular and Structural Biology, The Rockefeller University, New York, NY 10065.

The Journal of Cell Biology
|October 5, 2016
PubMed
Summary
This summary is machine-generated.

Nuclear pore complexes (NPCs) do not have a strict size limit for molecule passage. Instead, they act as a soft barrier, gradually impeding diffusion as molecule size increases.

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Area of Science:

  • Cell Biology
  • Biophysics

Background:

  • Nuclear pore complexes (NPCs) regulate transport between the nucleus and cytoplasm.
  • Passive diffusion through NPCs is traditionally believed to be limited by a sharp size threshold (30-60 kD).

Purpose of the Study:

  • To investigate the nature of the size barrier in NPCs for passive macromolecular diffusion.
  • To determine if a firm size threshold exists and characterize the barrier's properties.

Main Methods:

  • Thousands of in vivo time-resolved fluorescence microscopy measurements.
  • Brownian dynamics simulations.
  • Analysis of wild-type and mutant NPC strains with varying phenylalanine-glycine (FG) domain compositions.

Main Results:

  • NPCs lack a firm size threshold for passive diffusion; they present a soft barrier that intensifies with increasing molecular mass.
  • FG domains and diffusing macromolecules dynamically interact, creating entropic repulsion forces that constitute the soft barrier.
  • Specific FG domains near the cytoplasmic end, characterized by high net charge and low hydropathy, significantly obstruct passive diffusion.

Conclusions:

  • The NPC's barrier function is a gradual process, not a discrete size cutoff.
  • The dynamic interplay between FG domains and macromolecules shapes the NPC's permeability.
  • Functional compartmentalization exists within the NPC, with certain FG domains specialized for obstructing passive transport.