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Related Concept Videos

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...
Nuclear Export of mRNA02:31

Nuclear Export of mRNA

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...
Nuclear Export of mRNA02:31

Nuclear Export of mRNA

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...
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 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...
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 16, 2026

Analysis of mRNA Nuclear Export Kinetics in Mammalian Cells by Microinjection
11:32

Analysis of mRNA Nuclear Export Kinetics in Mammalian Cells by Microinjection

Published on: December 4, 2010

Nuclear export complexes in the frame.

Atlanta G Cook1, Elena Conti

  • 1MPI of Biochemistry, Am Klopferspitz 18, Martinsried, Germany. cook@biochem.mpg.de

Current Opinion in Structural Biology
|February 23, 2010
PubMed
Summary
This summary is machine-generated.

Karyopherin beta proteins mediate nuclear-cytoplasmic transport, regulated by Ran GTPase. RanGTP binding induces conformational changes, controlling cargo release for nuclear export and import.

More Related Videos

Single-Molecule Imaging of Nuclear Transport
12:13

Single-Molecule Imaging of Nuclear Transport

Published on: June 9, 2010

Related Experiment Videos

Last Updated: Jun 16, 2026

Analysis of mRNA Nuclear Export Kinetics in Mammalian Cells by Microinjection
11:32

Analysis of mRNA Nuclear Export Kinetics in Mammalian Cells by Microinjection

Published on: December 4, 2010

Single-Molecule Imaging of Nuclear Transport
12:13

Single-Molecule Imaging of Nuclear Transport

Published on: June 9, 2010

Area of Science:

  • Cellular biology
  • Molecular biology
  • Structural biology

Background:

  • Karyopherin beta proteins facilitate nuclear-cytoplasmic transport of proteins and RNA.
  • These transport factors utilize a HEAT-repeat architecture and are regulated by the GTPase Ran.
  • RanGTP functions as a nuclear compartment signal, influencing cargo binding to karyopherins.

Purpose of the Study:

  • To elucidate the structural mechanisms underlying nuclear export mediated by karyopherins.
  • To understand the impact of RanGTP binding on karyopherin structure and function.
  • To explore the role of cargo recognition in regulating macromolecule transport.

Main Methods:

  • Structural studies (e.g., X-ray crystallography, cryo-EM) were employed.
  • Biochemical assays were used to study protein-protein interactions.
  • Analysis of conformational changes induced by RanGTP binding.

Main Results:

  • RanGTP binding induces diverse conformational changes in karyopherins, from global to local.
  • These changes modulate the affinity of karyopherins for their cargo.
  • Structural insights into nuclear export mechanisms have been significantly advanced.
  • Cargo recognition acts as a surveillance mechanism for transport integrity.

Conclusions:

  • RanGTP binding is a key regulator of karyopherin-mediated nuclear transport.
  • Structural dynamics of karyopherins are critical for controlling cargo release and uptake.
  • The findings provide a deeper understanding of molecular transport regulation within the cell.