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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...
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...
Cytoskeletal Linker Proteins - Plakins01:09

Cytoskeletal Linker Proteins - Plakins

Plakins are large proteins with binding domains for microtubules, microfilaments, intermediate filaments, and membrane-associated protein complexes at cell junctions. Plakin functions are evolutionarily conserved and are primarily involved in organizing the different components of the cytoskeleton by crosslinking them to each other and connecting them to the cell-matrix and cell adhesion complexes. They are also known to interact with signal transducers, serve as scaffolds for signaling...
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...
Types of Intermediate Filaments01:31

Types of Intermediate Filaments

The intermediate filaments are an essential component of the cytoskeleton. Presently six types of intermediate filament have been identified. Type I and II are acidic and basic keratin proteins. Type III is of mesodermal origin and comprises four proteins: vimentin, desmin, glial fibrillary acidic protein (GFAP), and peripherin. Vimentin is commonly found in mesenchymal cells, desmin in muscle cells, GFAP in astrocytes, while peripherin is found in peripheral nervous system neurons (PNS). Type...

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Prelamin A in an <i>Lmna</i> <sup>L648R/L648R</sup> Mouse Model Does Not Promote Atherosclerosis or Vascular Smooth Muscle Loss.

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Farnesylated prelamin A induces fibroblast polarity defects in premature aging disorders by inhibiting nesprin-2-SUN2 LINC complex function.

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Prelamin A Does Not Promote Atherosclerosis or Vascular Smooth Muscle Loss.

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The nucleus activates mechano-responsiveness via FHOD-associated LINC complexes.

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

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Nuclear lamins and laminopathies.

Howard J Worman1

  • 1Departments of Medicine and of Pathology and Cell Biology, College of Physicians and Surgeons, Columbia University, New York, USA. hjw14@columbia.edu

The Journal of Pathology
|September 29, 2011
PubMed
Summary

Nuclear lamins are crucial for nuclear structure. Mutations in lamin genes cause laminopathies, a group of rare diseases, with ongoing research exploring treatment strategies.

Area of Science:

  • Cell Biology
  • Genetics
  • Biochemistry

Background:

  • Nuclear lamins form the nuclear lamina, essential for nuclear structure and mitosis.
  • Mutations in lamin genes, especially LMNA, cause diverse diseases known as laminopathies.
  • Lamins are ubiquitous in mammalian cells, yet laminopathies often exhibit tissue-specific effects.

Purpose of the Study:

  • To summarize current understanding of nuclear lamins and laminopathies.
  • To highlight the link between lamin gene mutations, nuclear morphology, and disease pathology.
  • To underscore the progress in identifying potential therapeutic strategies for laminopathies.

Main Methods:

  • Review of existing literature on nuclear lamins and laminopathies.
  • Analysis of studies investigating the impact of lamin mutations on nuclear structure.

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

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Detection of Nuclear Blebbing and DNA Leakage in Mammalian Cells by Immunofluorescence
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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
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Biophysical Assays to Probe the Mechanical Properties of the Interphase Cell Nucleus: Substrate Strain Application and Microneedle Manipulation

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  • Examination of research utilizing cellular and animal models for disease mechanism exploration.

    • Main Results:

    • Mutations in nuclear lamins lead to abnormalities in nuclear morphology.
    • The precise mechanisms linking nuclear structure alterations to disease pathology are still under investigation.
    • Basic research has identified promising avenues for treating rare laminopathies.

    Conclusions:

    • Nuclear lamins are critical structural proteins with implications in a spectrum of diseases.
    • Understanding the pathogenesis of laminopathies is advancing, offering hope for therapeutic development.
    • Further research in cellular and animal models is key to unlocking effective treatments for these rare genetic disorders.