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Related Concept Videos

Nuclear Protein Sorting01:34

Nuclear Protein Sorting

6.6K
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...
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Regulation of Nuclear Protein Sorting01:45

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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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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 Export of mRNA02:31

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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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Nuclear Export of mRNA02:31

Nuclear Export of mRNA

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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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Single-Molecule Imaging of Nuclear Transport
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A New Path through the Nuclear Pore.

Alejandro Gozalo1, Maya Capelson1

  • 1Department of Cell and Developmental Biology, Epigenetics Program, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.

Cell
|November 19, 2016
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Summary
This summary is machine-generated.

Researchers revealed the high-resolution structure of the nuclear pore-messenger RNA (mRNA) export complex. This finding challenges previous understandings of this crucial cellular gate and its role in nucleocytoplasmic transport.

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Area of Science:

  • Cell Biology
  • Structural Biology
  • Molecular Biology

Background:

  • The nuclear pore complex (NPC) regulates transport between the nucleus and cytoplasm.
  • Understanding NPC structure is key to deciphering nucleocytoplasmic communication pathways.
  • Existing models of the NPC may not fully represent its dynamic nature.

Purpose of the Study:

  • To determine the high-resolution structure of the cytoplasmic nuclear pore-mRNA export holo-complex.
  • To provide a detailed structural basis for mRNA export.
  • To challenge and refine current models of NPC architecture.

Main Methods:

  • Cryo-electron microscopy (Cryo-EM) was used to visualize the complex.
  • Advanced computational methods were employed for structural reconstruction.
  • Biochemical assays may have been used to validate the complex.

Main Results:

  • A high-resolution structure of the cytoplasmic nuclear pore-mRNA export holo-complex was obtained.
  • The structure reveals novel details about the NPC's cytoplasmic face during mRNA export.
  • The findings present a revised depiction of the NPC's architecture and function.

Conclusions:

  • The determined structure challenges textbook depictions of the nuclear pore complex.
  • This work offers new insights into the mechanism of mRNA export.
  • Accurate structural knowledge of the NPC is vital for understanding cellular transport processes.