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Related Concept Videos

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.
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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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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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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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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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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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Assay to Measure Nucleocytoplasmic Transport in Real Time within Motor Neuron-like NSC-34 Cells
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Phosphate-dependent nuclear export via a non-classical NES class recognized by exportin Msn5.

Ho Yee Joyce Fung1,2, Sanraj R Mittal3, Ashley B Niesman1,2

  • 1Department of Pharmacology, UT Southwestern Medical Center, Dallas, TX, 75039, US.

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Phosphorylation of the Pho4 transcription factor triggers its nuclear export via Msn5. Cryo-EM reveals how Pho4

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Structural Biology

Background:

  • Nuclear transport is critical for gene expression regulation.
  • Phosphorylation controls the localization of signaling proteins.
  • The yeast exportin Msn5 mediates nuclear export of phosphorylated cargo.

Purpose of the Study:

  • To elucidate the structural mechanism of Pho4 nuclear export by Msn5.
  • To characterize the phosphate-specific recognition mechanism.
  • To understand the regulation of Msn5 activity.

Main Methods:

  • High-resolution cryogenic-electron microscopy (cryo-EM).
  • Structural analysis of Pho4-Msn5 complex.

Main Results:

  • Determined the cryo-EM structure of phosphorylated Pho4's nuclear export signal bound to Msn5.
  • Identified specific interactions between Pho4 phospho-serines and Msn5 basic patches.
  • Revealed that Msn5 is autoinhibited in its unliganded state.
  • Demonstrated a phosphate-specific recognition mechanism distinct from classical signals.

Conclusions:

  • Pho4 nuclear export is mediated by a unique phosphorylation-dependent interaction with Msn5.
  • Msn5 autoinhibition explains cooperative binding and cytoplasmic release of Pho4.
  • This study expands the understanding of nuclear transport regulation by phosphorylation.