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Related Concept Videos

Nuclear Localization Signals and Import01:46

Nuclear Localization Signals and Import

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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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Directionality of Nuclear Transport01:42

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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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Nuclear Protein Sorting01:34

Nuclear Protein Sorting

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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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Nuclear Export01:42

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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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Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

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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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Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

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Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
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Single-Molecule Imaging of Nuclear Transport
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Transportin-1-dependent YB-1 nuclear import.

Daria A Mordovkina1, Ekaterina R Kim1, Ilya A Buldakov1

  • 1Institute of Protein Research, Russian Academy of Sciences, 4 Institutskaya St., 142290, Pushchino, Moscow Region, Russia.

Biochemical and Biophysical Research Communications
|November 6, 2016
PubMed
Summary

Transportin-1 is identified as the key protein mediating the nuclear import of the DNA/RNA-binding protein YB-1 (Y-box binding protein 1). This finding clarifies a crucial step in YB-1

Keywords:
Nuclear importTransportin-1YB-1

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Transport

Background:

  • The DNA/RNA-binding protein YB-1 (Y-box binding protein 1) has diverse functions in both cellular compartments.
  • YB-1 is typically found in the cytoplasm but can translocate to the nucleus under specific conditions.

Purpose of the Study:

  • To identify the transport factor responsible for mediating the nuclear import of YB-1.
  • To elucidate the mechanism of YB-1 nuclear translocation.

Main Methods:

  • Isolation of YB-1/transportin-1 complex from HeLa cell extract.
  • In vitro nuclear import assays using YB-1 and its mutants.
  • Inhibition studies using transportin-1 specific inhibitor M9M and importin β1 inhibitors.

Main Results:

  • The YB-1/transportin-1 complex was successfully isolated.
  • Nuclear import of YB-1 was inhibited by a transportin-1 inhibitor, but not by importin β1 inhibitors.
  • Mutations in the transportin-1-dependent nuclear localization signal abolished YB-1 transport.

Conclusions:

  • Transportin-1 is the primary mediator of YB-1 nuclear translocation.
  • This study identifies a novel role for transportin-1 in regulating YB-1 localization and function.