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Related Concept Videos

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...
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...
Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
The Nucleolus02:55

The Nucleolus

The nucleolus is the most prominent substructure of the nucleus. When it was first discovered, it was considered to be an isolated organelle that forms fibrils and granules. In 1931, the relationship between the nucleolus and chromosomes was first described by Heitz. He observed that the appearance and size of nucleolus varies depending on the stage of the cell cycle. He also noticed constricted regions on different chromosomes clustered together at definite cell cycle stages. These regions,...
Ribosomal RNA Synthesis02:53

Ribosomal RNA Synthesis

Ribosome synthesis is a highly complex and coordinated process involving more than 200 assembly factors. The synthesis and processing of ribosomal components occurs not only in the nucleolus but also in the nucleoplasm and the cytoplasm of eukaryotic cells.
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Related Experiment Video

Updated: Jul 11, 2026

Imaging Intranuclear Actin Rods in Live Heat Stressed Drosophila Embryos
07:57

Imaging Intranuclear Actin Rods in Live Heat Stressed Drosophila Embryos

Published on: May 15, 2020

Mechanisms underlying intranuclear rod formation.

Ana Domazetovska1, Biljana Ilkovski, Sandra T Cooper

  • 1Institute for Neuromuscular Research, Children's Hospital at Westmead, NSW, Australia.

Brain : a Journal of Neurology
|October 12, 2007
PubMed
Summary

Mutant alpha-skeletal actin (ACTA1) causes intranuclear rod myopathy (IRM) by forming nuclear actin aggregates. These aggregates impair cell division, contributing to muscle weakness.

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Validation of a Mouse Model to Disrupt LINC Complexes in a Cell-specific Manner
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Last Updated: Jul 11, 2026

Imaging Intranuclear Actin Rods in Live Heat Stressed Drosophila Embryos
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Published on: May 15, 2020

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

Area of Science:

  • Cell Biology
  • Muscle Physiology
  • Genetics

Background:

  • Intranuclear rod myopathy (IRM) is linked to ACTA1 mutations, forming nuclear actin aggregates.
  • The mechanisms of aggregate formation and their cellular impact in IRM remain unclear.

Purpose of the Study:

  • To investigate the formation and dynamics of intranuclear actin aggregates in IRM.
  • To elucidate the role of alpha-actinin in aggregate formation.
  • To determine the impact of intranuclear aggregates on cell function.

Main Methods:

  • Transfection of muscle and non-muscle cells with ACTA1 mutants (Val163Leu, Val163Met).
  • Live-cell imaging to observe aggregate formation and dynamics.
  • Analysis of alpha-actinin presence and influence.
  • Induction of cell stress to mimic pathogenic conditions.

Main Results:

  • Nuclear actin aggregates form within the nucleus and are dynamic structures.
  • Alpha-actinin influences actin organization within aggregates and is present in the nucleus.
  • Cell stress induces intranuclear aggregates similar to those in IRM.
  • Intranuclear actin aggregates reduce the mitotic index, impairing cell function.

Conclusions:

  • The nuclear environment facilitates actin polymerization and aggregate formation in IRM.
  • A common pathogenic mechanism involving intranuclear actin aggregates exists for IRM.
  • Intranuclear aggregates likely contribute to muscle weakness in IRM by affecting cell function.