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Related Concept Videos

Laminins are the Adhesive Proteins of Basal Lamina00:55

Laminins are the Adhesive Proteins of Basal Lamina

Laminins are heterotrimeric proteins with high molecular mass found in the extracellular matrix. Each laminin molecule is composed of three chains, viz. alpha, beta, and gamma, coded by five, four, and three paralogous genes, respectively. Laminins are categories based on the compositions of the three chains.
In humans, the five forms of alpha chains are LAMA 1, LAMA 2, LAMA 3, LAMA 4, and LAMA 5. The four forms of beta chains are LAMB 1, LAMB 2, LAMB 3, and LAMB 4. The three forms of gamma...
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...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
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...
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...

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Related Experiment Video

Updated: May 13, 2026

Detection of Nuclear Blebbing and DNA Leakage in Mammalian Cells by Immunofluorescence
06:23

Detection of Nuclear Blebbing and DNA Leakage in Mammalian Cells by Immunofluorescence

Published on: January 17, 2025

When lamins go bad: nuclear structure and disease.

Katherine H Schreiber1, Brian K Kennedy

  • 1Buck Institute for Research on Aging, Novato, CA 94945, USA.

Cell
|March 19, 2013
PubMed
Summary

Genetic mutations causing laminopathies lead to diverse disorders. Research is advancing understanding of nuclear structure

Area of Science:

  • Cell Biology
  • Genetics
  • Molecular Biology

Background:

  • Laminopathies are genetic disorders caused by mutations in nuclear lamins or nuclear envelope proteins.
  • These disorders present a wide range of symptoms, including muscular dystrophy, neuropathy, and premature aging syndromes.
  • The precise mechanisms underlying these diseases are still under investigation.

Purpose of the Study:

  • To summarize the current understanding of laminopathies and the biological roles of nuclear structure.
  • To highlight the association between nuclear envelope dysfunction and cellular abnormalities.
  • To introduce the potential of small molecules as therapeutic agents for laminopathies.

Main Methods:

  • Review of existing literature on laminopathies and nuclear structure.

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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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Biophysical Assays to Probe the Mechanical Properties of the Interphase Cell Nucleus: Substrate Strain Application and Microneedle Manipulation
16:27

Biophysical Assays to Probe the Mechanical Properties of the Interphase Cell Nucleus: Substrate Strain Application and Microneedle Manipulation

Published on: September 14, 2011

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Detection of Nuclear Blebbing and DNA Leakage in Mammalian Cells by Immunofluorescence
06:23

Detection of Nuclear Blebbing and DNA Leakage in Mammalian Cells by Immunofluorescence

Published on: January 17, 2025

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

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Biophysical Assays to Probe the Mechanical Properties of the Interphase Cell Nucleus: Substrate Strain Application and Microneedle Manipulation
16:27

Biophysical Assays to Probe the Mechanical Properties of the Interphase Cell Nucleus: Substrate Strain Application and Microneedle Manipulation

Published on: September 14, 2011

  • Analysis of the link between nuclear envelope dysfunction and cellular processes.
  • Identification of emerging therapeutic strategies.

    • Main Results:

    • Significant progress has been made in understanding laminopathies and nuclear structure biology.
    • Nuclear envelope dysfunction is linked to altered nuclear activity, impaired structural dynamics, and aberrant cell signaling.
    • Discovery of small molecules shows promise for future therapeutic interventions.

    Conclusions:

    • Mutations in nuclear lamins and related proteins cause diverse laminopathies.
    • Nuclear envelope integrity is crucial for normal cellular function.
    • Targeting nuclear envelope dysfunction with small molecules represents a promising therapeutic avenue.