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Nuclear Protein Sorting01:34

Nuclear Protein Sorting

6.5K
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...
6.5K
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 Export of mRNA02:31

Nuclear Export of mRNA

8.9K
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...
8.9K
Nucleosome Remodeling02:54

Nucleosome Remodeling

11.3K
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.
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
11.3K
Nuclear Export01:42

Nuclear Export

5.0K
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...
5.0K
Nuclear Localization Signals and Import01:46

Nuclear Localization Signals and Import

7.9K
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...
7.9K

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Related Experiment Video

Updated: Feb 19, 2026

Single-Molecule Imaging of Nuclear Transport
12:13

Single-Molecule Imaging of Nuclear Transport

Published on: June 9, 2010

13.8K

Nuclear pore complex plasticity during developmental process as revealed by super-resolution microscopy.

Julien Sellés1,2, May Penrad-Mobayed2, Cyndélia Guillaume1

  • 1Matière et Systèmes Complexes, Université Paris Diderot/CNRS (UMR 7057), 75205, Paris, Cedex 13, France.

Scientific Reports
|November 9, 2017
PubMed
Summary

Nuclear Pore Complex (NPC) structure changes during oocyte development. Researchers used dSTORM microscopy to observe decreased NPC density and a more ordered lattice structure in Xenopus laevis oocytes.

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3D Multicolor DNA FISH Tool to Study Nuclear Architecture in Human Primary Cells
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3D Multicolor DNA FISH Tool to Study Nuclear Architecture in Human Primary Cells
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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Microscopy

Background:

  • The Nuclear Pore Complex (NPC) is crucial for regulating molecular transport between the nucleus and cytoplasm.
  • Understanding nuclear pore plasticity, or how NPC structure changes with physiological cues, is vital for comprehending cellular selectivity.
  • Oocyte development involves significant cellular remodeling, potentially impacting NPC organization.

Purpose of the Study:

  • To investigate the impact of oocyte development on the internal structure and large-scale organization of the Nuclear Pore Complex (NPC).
  • To analyze changes in NPC dimensions and arrangement during Xenopus laevis oocyte maturation.

Main Methods:

  • Utilized direct Stochastic Optical Reconstruction Microscopy (dSTORM), an optical super-resolution technique.
  • Employed staining for FG-Nups and gp210 proteins to visualize NPC components.
  • Applied autocorrelation image processing to measure NPC diameters.
  • Analyzed NPC distribution using angular and radial density functions.

Main Results:

  • Observed a decrease in the global diameter of the NPC, including the central channel and luminal ring.
  • Demonstrated a progressive decrease in NPC density during Xenopus laevis oocyte development.
  • Revealed an ordering of NPCs into a square lattice structure as oocytes develop.

Conclusions:

  • Oocyte development significantly alters Nuclear Pore Complex structure and organization.
  • NPCs become smaller and more regularly spaced in developing oocytes.
  • These findings contribute to understanding nuclear pore plasticity and its role in cellular processes.