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Related Concept Videos

Nuclear Export01:42

Nuclear Export

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...
Nuclear Protein Sorting01:34

Nuclear Protein Sorting

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...
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

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...
Additional Subnuclear Structures02:10

Additional Subnuclear Structures

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, paraspeckles, etc. These nuclear...
Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
Nuclear Export of mRNA02:31

Nuclear Export of mRNA

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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Related Experiment Video

Updated: May 10, 2026

Validation of a Mouse Model to Disrupt LINC Complexes in a Cell-specific Manner
09:02

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

Published on: December 10, 2015

Nesprins: from the nuclear envelope and beyond.

Dipen Rajgor1, Catherine M Shanahan

  • 1James Black Centre, Cardiovascular Division, King's College London, 125 Coldharbour lane, London SE5 9NU, UK.

Expert Reviews in Molecular Medicine
|July 9, 2013
PubMed
Summary
This summary is machine-generated.

Nuclear envelope spectrin-repeat proteins (Nesprins) are crucial intracellular scaffolds. Mutations in these proteins disrupt tissue-specific scaffolds, potentially explaining diseases like laminopathies.

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A Protocol for Using F&#246;rster Resonance Energy Transfer (FRET)-force Biosensors to Measure Mechanical Forces across the Nuclear LINC Complex
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A Protocol for Using Förster Resonance Energy Transfer (FRET)-force Biosensors to Measure Mechanical Forces across the Nuclear LINC Complex

Published on: April 11, 2017

Related Experiment Videos

Last Updated: May 10, 2026

Validation of a Mouse Model to Disrupt LINC Complexes in a Cell-specific Manner
09:02

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

Published on: December 10, 2015

A Protocol for Using F&#246;rster Resonance Energy Transfer (FRET)-force Biosensors to Measure Mechanical Forces across the Nuclear LINC Complex
09:43

A Protocol for Using Förster Resonance Energy Transfer (FRET)-force Biosensors to Measure Mechanical Forces across the Nuclear LINC Complex

Published on: April 11, 2017

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Nuclear envelope spectrin-repeat proteins (Nesprins) are a novel protein family.
  • Initially identified at the nuclear envelope (NE), nesprins connect the nucleus to the cytoskeleton.
  • Nesprins comprise diverse, tissue-specific isoforms localizing to multiple subcellular compartments.

Purpose of the Study:

  • To describe the essential roles of nesprins in maintaining cellular architecture.
  • To explore how nesprins function as scaffolds and linkers at the NE and other cellular domains.
  • To investigate the link between nesprin mutations, disrupted tissue-specific scaffolds, and associated diseases.

Main Methods:

  • Literature review and synthesis of existing research on nesprin function and localization.
  • Analysis of data linking nesprin structure and function to cellular architecture.
  • Speculative analysis of mutation impacts on nesprin scaffolds and disease etiology.

Main Results:

  • Nesprins are essential for maintaining cellular architecture through scaffolding and linking functions.
  • Nesprins operate at the nuclear envelope and other subcellular locations.
  • Nesprin isoforms exhibit tissue-specific expression and localization patterns.

Conclusions:

  • Nesprins are vital for cellular structure and integrity.
  • Disruptions in tissue-specific nesprin scaffolds due to mutations are implicated in diseases.
  • Understanding nesprin function is key to deciphering the tissue-specific nature of nesprin-associated disorders like laminopathies.