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Related Concept Videos

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.
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

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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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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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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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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
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Related Experiment Video

Updated: May 22, 2025

Using SecM Arrest Sequence as a Tool to Isolate Ribosome Bound Polypeptides
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An ER-associated structure sequesters misassembled FG-rich nucleoporins to help maintain nuclear pore complex

Madison Pletan1,2, Emily Wang1, Luke Gohmann1,2

  • 1Department of Cell and Developmental Biology, University of Michigan Medical School, Ann Arbor, MI 48104, USA.

Journal of Cell Science
|March 13, 2025
PubMed
Summary

The endoplasmic reticulum (ER) sequesters misassembled nucleoporins (Nups) in ER foci, preventing nuclear pore complex (NPC) dysfunction. This ER sequestration mechanism is crucial for maintaining nucleo-cytoplasmic transport and may impact neurodegenerative diseases.

Keywords:
Endoplasmic reticulumNuclear membrane transportProtein quality contro

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Validation of a Mouse Model to Disrupt LINC Complexes in a Cell-specific Manner
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Validation of a Mouse Model to Disrupt LINC Complexes in a Cell-specific Manner

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Neuroscience

Background:

  • Nucleoporins (Nups) are essential for nuclear pore complex (NPC) assembly and function.
  • Misassembly and mislocalization of Nups outside the nuclear envelope are linked to cellular dysfunction and neurodegenerative diseases.

Purpose of the Study:

  • To investigate the fate and cellular consequences of mislocalized nucleoporins (Nups).
  • To understand the mechanisms by which the cell manages misassembled Nups.
  • To explore the potential role of these mechanisms in age-related neurodegenerative diseases.

Main Methods:

  • Depletion of the structural nucleoporin Nup98 to induce Nup misassembly.
  • Microscopy to observe the localization and formation of misassembled Nups.
  • Genetic and molecular approaches to identify proteins involved in the sequestration process.

Main Results:

  • Misassembled phenylalanine-glycine-rich Nups (FG-Nups) accumulate in discrete structures within the endoplasmic reticulum (ER), termed ER foci.
  • Formation of these ER foci requires ER morphogenic proteins (RTN3, ATL3, LNP) and the kinesin-1 motor.
  • Preventing ER foci formation leads to impaired NPC nucleo-cytoplasmic transport, suggesting ER sequestration is protective.

Conclusions:

  • The endoplasmic reticulum acts as a compartment to sequester misassembled Nups, thereby maintaining nuclear pore complex (NPC) function.
  • This ER sequestration pathway is essential for cellular homeostasis and preventing disruption of nucleo-cytoplasmic transport.
  • Understanding this mechanism provides insights into the molecular basis of neurodegenerative diseases associated with Nup mislocalization.