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Related Concept Videos

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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.
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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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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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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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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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Updated: Oct 13, 2025

Single-Molecule Imaging of Nuclear Transport
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Nuclear pores dilate and constrict in cellulo.

Christian E Zimmerli1,2,3, Matteo Allegretti1,3, Vasileios Rantos4,5

  • 1Structural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), 69117 Heidelberg, Germany.

Science (New York, N.Y.)
|November 11, 2021
PubMed
Summary

Nuclear pore complexes (NPCs) dynamically change size. In growing cells, NPCs dilate, but constrict under stress, revealing a link between nuclear envelope tension and NPC conformation.

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Area of Science:

  • Cell Biology
  • Structural Biology
  • Biophysics

Background:

  • Nuclear pore complexes (NPCs) are crucial for nucleocytoplasmic transport in eukaryotic cells.
  • NPCs form a cylindrical structure from ~30 nucleoporins, regulating molecular traffic between the nucleus and cytoplasm.
  • The dynamic nature and conformational variations of NPCs are not fully understood.

Purpose of the Study:

  • To investigate the large-scale conformational changes of NPCs in living cells.
  • To elucidate the molecular mechanisms and physiological conditions governing NPC size variations.
  • To establish a link between nuclear envelope membrane tension and NPC structure.

Main Methods:

  • Cryo-electron tomography was employed to visualize NPCs in situ.
  • Integrative structural modeling was used to reconstruct NPC conformations.
  • Cellular conditions such as exponential growth, energy depletion, and osmotic stress were applied.

Main Results:

  • NPCs in exponentially growing cells exhibited a dilated conformation.
  • NPCs reversibly constricted under conditions of cellular energy depletion and hypertonic osmotic stress.
  • These findings suggest that NPC conformation is sensitive to cellular physiological states.

Conclusions:

  • The study reveals that NPC diameter is not static and varies with cellular conditions.
  • A model is proposed where nuclear envelope membrane tension influences NPC conformation.
  • This provides new insights into the dynamic regulation of nucleocytoplasmic transport.