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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

Nuclear Export

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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.
NES are of three types- the canonical 10-residue long leucine-rich signal and other...
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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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Directionality of Nuclear Transport01:42

Directionality of Nuclear Transport

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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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Nuclear Export of mRNA02:31

Nuclear Export of mRNA

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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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Related Experiment Video

Updated: Oct 17, 2025

Measuring Nucleotide Binding to Intact, Functional Membrane Proteins in Real Time
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Measuring Nucleotide Binding to Intact, Functional Membrane Proteins in Real Time

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Characterizing Binding Interactions That Are Essential for Selective Transport through the Nuclear Pore Complex.

Kathleen M Lennon1, Mohammad Soheilypour2, Mohaddeseh Peyro2

  • 1Department of Molecular Medicine, Beckman Research Institute of the City of Hope Comprehensive Cancer Center, Duarte, CA 91010, USA.

International Journal of Molecular Sciences
|October 13, 2021
PubMed
Summary
This summary is machine-generated.

Researchers studied nuclear transport receptor (NTR) interactions with FG Nups, key to nuclear pore complex (NPC) selectivity. Findings reveal binding is negatively cooperative and density-dependent, advancing understanding of nucleocytoplasmic transport mechanisms.

Keywords:
FG NupsNPC barrier mimicagent-based modelingmolecular dynamicsnuclear pore complexnuclear transport receptorssingle molecule localization microscopy (SMLM)

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

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Related Experiment Videos

Last Updated: Oct 17, 2025

Measuring Nucleotide Binding to Intact, Functional Membrane Proteins in Real Time
08:33

Measuring Nucleotide Binding to Intact, Functional Membrane Proteins in Real Time

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Single-Molecule Imaging of Nuclear Transport
12:13

Single-Molecule Imaging of Nuclear Transport

Published on: June 9, 2010

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Area of Science:

  • Cell Biology
  • Biophysics
  • Molecular Biology

Background:

  • Nuclear pore complex (NPC) regulates transport between nucleus and cytoplasm.
  • Nuclear transport receptors (NTRs) mediate selective macromolecule transport via FG Nup interactions.

Purpose of the Study:

  • To investigate the binding interactions between NTRs and FG Nups in vitro.
  • To develop and utilize an NPC barrier mimic for studying these interactions.

Main Methods:

  • Created a stationary phase with yeast FG Nup (Nsp1) fragments on glass coverslips.
  • Used a mobile phase containing nuclear transport factor 2 (NTF2) and other NTRs.
  • Combined experimental binding assays with molecular dynamics simulations and agent-based modeling.

Main Results:

  • Binding was influenced by FG repeat number, charge, and fragment density in the stationary phase.
  • Avidity, nonspecific proteins, and additional NTRs affected binding in the mobile phase.
  • NTF2 binding to Nsp1FG demonstrated negative cooperativity and density dependence.

Conclusions:

  • Experimental and computational modeling approaches effectively interrogate NPC-mediated transport.
  • Binding characteristics of NTRs and FG Nups are crucial for maintaining NPC selectivity.
  • Findings provide insights into the physical principles governing nucleocytoplasmic transport.