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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...
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...
Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
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...

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Related Experiment Video

Updated: Jun 1, 2026

Single-Molecule Imaging of Nuclear Transport
12:13

Single-Molecule Imaging of Nuclear Transport

Published on: June 9, 2010

Lighting up the nuclear pore complex.

Martin Kahms1, Jana Hüve, Ramona Wesselmann

  • 1Institute of Medical Physics and Biophysics, and Center for Nanotechnology (CeNTech), University of Muenster, Heisenbergstrasse 11, 48149 Muenster, Germany.

European Journal of Cell Biology
|June 3, 2011
PubMed
Summary
This summary is machine-generated.

Nuclear pore complex (NPC) transport relies on FG-domains, but translocation mechanisms remain debated. This review explores FG-domain arrangement and optical methods for analyzing NPC gating and transport selectivity.

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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

Related Experiment Videos

Last Updated: Jun 1, 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
  • Biophysics

Background:

  • Nuclear pore complex (NPC) transport is crucial for cellular function.
  • Transport involves phenylalanine-glycine rich domains (FG-domains) interacting with nuclear transport receptors (NTRs).
  • The precise mechanism for fast and selective translocation through the NPC is still under investigation.

Purpose of the Study:

  • To review current models of NPC transport.
  • To summarize recent findings on NPC translocation using super-resolution microscopy.
  • To discuss the potential of optical methods for analyzing NPC structure and function.

Main Methods:

  • Review of existing literature and transport models.
  • Analysis of super-resolution microscopy data on NPC translocation.
  • Discussion of optical techniques for NPC studies.

Main Results:

  • FG-domains are key docking sites for NTRs and cargo.
  • High-speed and selective transport mechanisms within the NPC are not fully understood.
  • Super-resolution microscopy provides new insights into FG-domain organization and transport.

Conclusions:

  • Understanding FG-domain molecular arrangement is vital for deciphering NPC gating.
  • Optical methods, particularly super-resolution microscopy, are powerful tools for studying the NPC.
  • Further research using advanced optical techniques will illuminate NPC transport dynamics and selectivity.