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Related Concept Videos

Nuclear Protein Sorting01:34

Nuclear Protein Sorting

6.5K
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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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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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 Export of mRNA02:31

Nuclear Export of mRNA

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Nuclear Localization Signals and Import01:46

Nuclear Localization Signals and Import

8.0K
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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Updated: Feb 28, 2026

Spatiotemporally Controlled Nuclear Translocation of Guests in Living Cells Using Caged Molecular Glues as Photoactivatable Tags
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O-GlcNAc-ylation in the Nuclear Pore Complex.

Andrew Ruba1, Weidong Yang1

  • 1Department of Biology, Temple University, Philadelphia, PA.

Cellular and Molecular Bioengineering
|June 23, 2017
PubMed
Summary

O-GlcNAc-ylation modifies nuclear pore complex (NPC) proteins, influencing transport. This review explores O-GlcNAc

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • O-GlcNAc-ylation is a post-translational modification adding O-linked β-N-acetylglucosamine to serine/threonine residues.
  • Nuclear Pore Complex (NPC) proteins, particularly intrinsically disordered nucleoporins (Nups) with FG repeats, are heavily O-GlcNAc-ylated.
  • O-GlcNAc modification is implicated in forming the NPC's selectivity barrier for nucleocytoplasmic transport.

Purpose of the Study:

  • To review current knowledge on O-GlcNAc-ylated Nups.
  • To highlight novel techniques for studying O-GlcNAc roles in the NPC.
  • To propose a new model for O-GlcNAc's impact on NPC permeability.

Main Methods:

  • Literature review of O-GlcNAc-ylation and NPC function.
  • Discussion of emerging experimental techniques (e.g., mass spectrometry, genetic manipulation).
Keywords:
glycosylationnuclear pore complexnucleoporins

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Heterokaryon Technique for Analysis of Cell Type-specific Localization
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Heterokaryon Technique for Analysis of Cell Type-specific Localization

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  • Conceptual modeling of O-GlcNAc's structural and functional contributions.
  • Main Results:

    • O-GlcNAc modification is prevalent on FG-Nups within the NPC.
    • The density of O-GlcNAc correlates with the NPC's selectivity barrier function.
    • Existing data suggest O-GlcNAc influences Nup structure and NPC transport dynamics.

    Conclusions:

    • O-GlcNAc-ylation plays a critical, yet not fully understood, role in NPC structure and function.
    • Further research using advanced techniques is needed to elucidate these roles.
    • A new model is proposed to explain O-GlcNAc's effect on NPC permeability.