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Related Concept Videos

Nuclear Protein Sorting01:34

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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 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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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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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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Single-Molecule Imaging of Nuclear Transport
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The Nuclear Pore Complex as a Flexible and Dynamic Gate.

Kevin E Knockenhauer1, Thomas U Schwartz1

  • 1Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.

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|March 12, 2016
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Summary
This summary is machine-generated.

Nuclear pore complexes (NPCs) are crucial for transport between the nucleus and cytoplasm. Their structural flexibility and heterogeneity are key to understanding NPC assembly and function.

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Area of Science:

  • Cell Biology
  • Structural Biology
  • Biochemistry

Background:

  • Nuclear pore complexes (NPCs) regulate molecular traffic between the nucleus and cytoplasm.
  • NPCs are large protein assemblies forming gates in the nuclear envelope.
  • Understanding NPC structure is vital for cell function.

Purpose of the Study:

  • To review the current understanding of nuclear pore complex research.
  • To focus on the functional implications of NPC structural and compositional heterogeneity.
  • To explore the role of flexibility in NPC assembly and function.

Main Methods:

  • Literature review of current NPC research.
  • Analysis of structural and compositional data.
  • Discussion of functional implications.

Main Results:

  • NPCs consist of scaffold components and disordered elements forming a selective barrier.
  • Structural elements of NPCs exhibit flexibility.
  • Heterogeneity in NPC structure and composition impacts function.

Conclusions:

  • NPC structural flexibility is important for assembly and function.
  • Understanding NPC heterogeneity provides insights into nuclear transport.
  • Further research into NPC structure-function relationships is warranted.