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Related Concept Videos

Nuclear Protein Sorting01:34

Nuclear Protein Sorting

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...
Directionality of Nuclear Transport01:42

Directionality of Nuclear Transport

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...
Nuclear Export01:42

Nuclear Export

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...
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

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...
Nuclear Localization Signals and Import01:46

Nuclear Localization Signals and Import

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...
Overview of Protein Sorting and Transport01:45

Overview of Protein Sorting and Transport

Eukaryotic cells have different membrane-bound organelles with distinct protein requirements. The process by which proteins are targeted to a specific organelle is called protein sorting.
Protein sorting can be of two types: signal-based sorting and vesicle-based trafficking. In signal-based sorting, specific amino acid sequences called sorting signals target proteins to the proper location inside the cell either via gated transport or by protein translocation.  In gated transport, folded...

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Related Experiment Video

Updated: May 16, 2026

Single-Molecule Imaging of Nuclear Transport
12:13

Single-Molecule Imaging of Nuclear Transport

Published on: June 9, 2010

Nuclear transport: beginning to gel?

Maureen A Powers1, Douglass J Forbes

  • 1Department of Cell Biology, Emory University School of Medicine, Atlanta, GA 30322, USA. mpowers@emory.edu

Current Biology : CB
|December 11, 2012
PubMed
Summary
This summary is machine-generated.

This study uses reconstituted nuclei and recombinant proteins to investigate the nuclear pore complex, moving beyond theoretical predictions to biochemical certainty in understanding nucleocytoplasmic transport.

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Spatiotemporally Controlled Nuclear Translocation of Guests in Living Cells Using Caged Molecular Glues as Photoactivatable Tags
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Spatiotemporally Controlled Nuclear Translocation of Guests in Living Cells Using Caged Molecular Glues as Photoactivatable Tags

Published on: January 17, 2019

Related Experiment Videos

Last Updated: May 16, 2026

Single-Molecule Imaging of Nuclear Transport
12:13

Single-Molecule Imaging of Nuclear Transport

Published on: June 9, 2010

Spatiotemporally Controlled Nuclear Translocation of Guests in Living Cells Using Caged Molecular Glues as Photoactivatable Tags
10:10

Spatiotemporally Controlled Nuclear Translocation of Guests in Living Cells Using Caged Molecular Glues as Photoactivatable Tags

Published on: January 17, 2019

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The nuclear pore complex (NPC) is a large protein assembly essential for regulating transport between the nucleus and cytoplasm.
  • Understanding the precise mechanisms of NPC-mediated transport has been challenging, relying heavily on predictive models.
  • Key questions remain regarding how NPCs handle diverse cargo, from small molecules to large viral genomes.

Purpose of the Study:

  • To biochemically test existing mechanistic predictions of nuclear pore complex function.
  • To elucidate the mechanisms governing nucleocytoplasmic transport of various cargoes.
  • To provide a more certain, experimentally validated understanding of NPC activity.

Main Methods:

  • Utilized in vitro reconstituted nuclei for controlled experimental conditions.
  • Employed recombinant proteins to specifically probe NPC components and interactions.
  • Combined biochemical assays with structural analysis to validate functional predictions.

Main Results:

  • Demonstrated the productive testing of mechanistic predictions regarding NPC function.
  • Provided biochemical evidence supporting specific models of nucleocytoplasmic transport.
  • Successfully reconstituted and analyzed NPC-mediated traffic in a controlled system.

Conclusions:

  • The combination of reconstituted systems and recombinant proteins offers a powerful approach to dissecting complex molecular machinery like the NPC.
  • This study moves the field from theoretical prediction towards experimental validation of NPC mechanisms.
  • Findings contribute to a more certain understanding of how the nuclear pore complex mediates essential cellular transport processes.