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Related Concept Videos

Nuclear Protein Sorting01:34

Nuclear Protein Sorting

4.7K
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

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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Nuclear Export of mRNA02:31

Nuclear Export of mRNA

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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 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.
NES are of three types- the canonical 10-residue long leucine-rich signal and other...
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Additional Subnuclear Structures02:10

Additional Subnuclear Structures

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The eukaryotic nucleus is a double membrane-bound organelle that contains nearly all of the cell’s genetic material in the form of chromosomes. It is rightly called the “brain” of the cell as it shoulders the responsibility of responding to various physiological processes, stress, altered metabolic conditions, and other cellular signals. 
The nucleus contains many membrane-less subnuclear organelles or nuclear bodies, such as nucleoli, Cajal bodies, speckles,...
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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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Single-Molecule Imaging of Nuclear Transport

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Structure and Function of the Nuclear Pore Complex.

Stefan Petrovic1, George W Mobbs1, Christopher J Bley1

  • 1Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California 91125, USA.

Cold Spring Harbor Perspectives in Biology
|September 12, 2022
PubMed
Summary
This summary is machine-generated.

Researchers determined the near-atomic structure of the human nuclear pore complex (NPC), a vital protein channel. This breakthrough advances understanding of genetic information flow, mRNA export, and related diseases.

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Last Updated: Aug 29, 2025

Single-Molecule Imaging of Nuclear Transport
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Published on: June 9, 2010

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Area of Science:

  • Cell Biology
  • Structural Biology
  • Molecular Biology

Background:

  • The nucleus houses eukaryotic genomes within a double membrane, connected to the endoplasmic reticulum.
  • The nuclear pore complex (NPC) is a large, multi-protein channel regulating transport across the nuclear envelope.
  • Understanding NPC structure is crucial for comprehending gene expression and cellular function.

Purpose of the Study:

  • To present the near-atomic composite structure of the human NPC.
  • To highlight advancements in determining the structure of large, complex molecular machines.
  • To establish a foundation for studying NPC-related biological processes and diseases.

Main Methods:

  • Integration of biochemical reconstitution with cryo-electron tomography.
  • Docking high-resolution structures of NPC subcomplexes into tomographic reconstructions.
  • Biochemical and physiological validation of structural findings.

Main Results:

  • Determination of the near-atomic structure of the human NPC.
  • Overcoming previous limitations in resolving the structure of large, dynamic complexes.
  • Providing a structural framework for key cellular transport mechanisms.

Conclusions:

  • The near-atomic structure of the human NPC is a significant milestone.
  • This structural understanding facilitates research into mRNA export and NPC-associated diseases.
  • The human NPC structure serves as a model for studying other large molecular assemblies.