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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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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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Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
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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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Ras-related nuclear protein or Ran is a small G protein that cycles between its GTP and GDP bound states. Ran specific regulators, a Ran GTPase Activating Protein or RanGAP present in the cytosol and a Ran guanine nucleotide exchange factor or RanGEF present inside the nucleus regulate GTP/GDP exchange. A high concentration of GTP inside the cells, in addition to this asymmetric distribution of  Ran-specific regulators, leads to a higher RanGTP concentration inside the nucleus. This...
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Updated: Nov 25, 2025

Single-Molecule Imaging of Nuclear Transport
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Dissecting the Structural Dynamics of the Nuclear Pore Complex.

Zhanna Hakhverdyan1, Kelly R Molloy2, Sarah Keegan3

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

Molecular Cell
|December 17, 2020
PubMed
Summary

Researchers studied the dynamics of the nuclear pore complex (NPC) in yeast. They found that while all proteins (Nups) turn over slowly, their exchange rates depend on structural roles, not transport function, revealing NPC resilience.

Keywords:
assemblydynamicsexchangenuclear pore complexnucleoporinquantitative proteomicsturnover

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Proteomics

Background:

  • Macromolecular assemblies are crucial for cellular processes and are often dynamic.
  • The nuclear pore complex (NPC) is a large assembly regulating transport between the nucleus and cytoplasm.
  • Understanding the dynamics of NPC components is essential for comprehending nuclear transport and cellular function.

Purpose of the Study:

  • To develop a proteomics method for comprehensively analyzing yeast NPC component dynamics.
  • To investigate the turnover and exchange rates of various nucleoporins (Nups).
  • To determine factors influencing Nup dynamics, such as position, accessibility, transport role, and structural function.

Main Methods:

  • Development of a novel proteomics approach.
  • Quantitative analysis of yeast NPC component turnover.
  • Correlation analysis between Nup exchange rates and their structural/functional properties.

Main Results:

  • All Nups exhibit slow turnover, but their exchange rates vary significantly.
  • Nup exchange rates are primarily correlated with their structural role (scaffold vs. connector), not their position, accessibility, or transport function.
  • Targeted perturbations demonstrated the NPC's dynamic resilience to structural damage.

Conclusions:

  • NPC component dynamics are primarily dictated by structural organization rather than transport activity.
  • The NPC possesses inherent resilience, adapting to perturbations through dynamic component exchange.
  • This study provides new insights into the dynamic nature of macromolecular assemblies like the NPC.