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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 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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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 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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The selective permeability barrier in the nuclear pore complex.

Christina Li1, Alexander Goryaynov1, Weidong Yang1

  • 1a Department of Biology , Temple University , Philadelphia , PA , USA.

Nucleus (Austin, Tex.)
|September 28, 2016
PubMed
Summary

Researchers used super-resolution microscopy to study the nuclear pore complex (NPC) barrier, revealing how intrinsically disordered phenylalanine-glycine-rich nucleoporins (FG-Nups) control transport and how nuclear transport receptors (NTRs) compete for passage.

Keywords:
Nucleoporinsintrinsically disordered proteinsnucleocytoplasmic transportsuper-resolution fluorescence microcopy

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biophysics

Background:

  • The nuclear pore complex (NPC) regulates macromolecule transport between the nucleus and cytoplasm in eukaryotes.
  • A permeability barrier formed by phenylalanine-glycine-rich nucleoporins (FG-Nups) governs selective nucleocytoplasmic transport.
  • Large cargo molecules require nuclear transport receptors (NTRs) to navigate the FG-Nup barrier via facilitated diffusion.

Purpose of the Study:

  • To investigate the native structure and conformation of the FG-Nups permeability barrier within NPCs.
  • To elucidate the competitive interactions among multiple NTRs engaging with the FG-Nups barrier.
  • To address fundamental questions regarding the configuration and function of the FG-Nups barrier in native NPCs.

Main Methods:

  • Application of high-speed super-resolution fluorescence microscopy.
  • In situ mapping of the natural structure of the FG-Nups barrier.
  • Determination of competitive binding dynamics between multiple NTRs and the FG-Nups barrier.

Main Results:

  • Detailed mapping of the FG-Nups barrier's natural structure in native NPCs.
  • Quantification of the competition dynamics among various NTRs interacting with the FG-Nups barrier.
  • New evidence clarifying the configuration and functional mechanisms of the FG-Nups barrier.

Conclusions:

  • The study provides novel insights into the structural organization of the FG-Nups barrier.
  • Understanding NTR competition is crucial for comprehending nucleocytoplasmic transport regulation.
  • Recent findings advance the field's understanding of NPC function and transport selectivity.