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Related Concept Videos

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...
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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.
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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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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.
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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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Single-Molecule Imaging of Nuclear Transport
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RNA export mediated by tap involves NXT1-dependent interactions with the nuclear pore complex.

L Lévesque1, B Guzik, T Guan

  • 1Center for Cell Signaling, Department of Biochemistry, University of Virginia, Charlottesville, Virginia 22908, USA.

The Journal of Biological Chemistry
|October 2, 2001
PubMed
Summary
This summary is machine-generated.

Nuclear export receptor NXT1 (Nuclear export transporter 1) partners with Tap to bind nucleoporins, facilitating RNA translocation through the nuclear pore complex. This interaction is crucial for efficient viral mRNA export in vivo.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Virology

Background:

  • Nuclear export of ribonucleoprotein complexes is essential for cellular function.
  • This process relies on cis-acting signals and receptor-mediated translocation through the nuclear pore complex.
  • The Tap protein is known to be involved in the export of specific viral RNAs.

Purpose of the Study:

  • To characterize the function of NXT1 in the Tap-dependent RNA export pathway.
  • To investigate the role of NXT1 in the interaction between Tap-RNA complexes and nucleoporins.
  • To elucidate the mechanism of nuclear export for intron-containing viral mRNA.

Main Methods:

  • In vitro binding assays using recombinant proteins to study Tap-RNA-nucleoporin interactions.
  • Mutational analysis to assess the necessity of specific interactions for nuclear export in vivo.
  • Reconstitution of nucleoporin binding using purified proteins.

Main Results:

  • NXT1 stimulates the binding of Tap-RNA complexes to nucleoporins in vitro.
  • Mutational analysis confirmed the necessity of these interactions for in vivo viral mRNA export.
  • Tap protein possesses distinct domains for binding nucleoporins and NXT1, both vital for export.
  • RNA export is mediated by a Tap-NXT1 heterodimer, with NXT1 regulating Tap-RNA complex affinity for nucleoporins.
  • NXT1-dependent binding to the nucleoporin p62 was reconstituted in vitro, representing a step in translocation.

Conclusions:

  • NXT1 is a critical component of the Tap-dependent RNA export pathway.
  • NXT1 functions by modulating the affinity of the Tap-RNA complex for nucleoporins, thereby regulating nuclear pore complex translocation.
  • The study proposes a model where NXT1-mediated binding to p62 is a key step in the nuclear export process.