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The basal lamina is a thin extracellular layer that lies underneath the cells and separates them from other tissues. The three layers of the basal lamina are lamina lucida, lamina densa and lamina reticularis. The basal lamina, a mixture of glycoproteins and collagen, provides an attachment site for the epithelium, separating it from underlying connective tissue. The framework of basal lamina has other essential proteins such as laminins mesh, perlecan, entactin, and type IV collagen.
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Cells migrating in response to external stimuli form lamellipodia, which are thin membrane protrusions supported by a mesh of linked, branched, or unbranched actin filaments. These actin filaments interact with myosin motor proteins, creating the dynamic actomyosin complex within the cytoskeleton. Contractility, or the ability to generate contractile stress, is inherent to the actomyosin complex. It helps cells detect the stiffness of the surrounding ECM and exert contractile force for...
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Lamins as structural nuclear elements through evolution.

Jacob Odell1, Jan Lammerding2

  • 1Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY 14853, USA; Graduate Field of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, NY 14853, USA.

Current Opinion in Cell Biology
|October 23, 2023
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Summary
This summary is machine-generated.

Lamins are nuclear proteins crucial for nuclear structure and gene regulation in vertebrates. Studying lamin homologs in simpler organisms like amoebas offers evolutionary insights and may reveal new functions of vertebrate lamins.

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Area of Science:

  • Cell Biology
  • Evolutionary Biology
  • Biochemistry

Background:

  • Lamins are nuclear intermediate filament proteins essential for nuclear mechanics, chromatin organization, and gene expression in vertebrates.
  • Key lamin functions are conserved in homologs found in basal metazoans such as Drosophila and Caenorhabditis elegans.

Purpose of the Study:

  • To investigate the functional comparison of lamin homologs in non-metazoan organisms, specifically Dictyostelium discoideum, with their metazoan counterparts.
  • To enhance understanding of eukaryotic evolution through the study of distantly related lamins.
  • To explore potential new insights into vertebrate lamin functions derived from non-metazoan homologs.

Main Methods:

  • Comparative analysis of lamin protein sequences and structures.
  • Functional assays in model organisms (e.g., Dictyostelium, C. elegans, Drosophila).
  • Nuclear envelope protein interaction studies.

Main Results:

  • Identification and characterization of lamin homologs in non-metazoan eukaryotes.
  • Initial functional comparisons revealing conserved and divergent roles.
  • Evidence suggesting evolutionary conservation of some lamin functions across eukaryotes.

Conclusions:

  • Lamins represent an ancient protein family with roles predating metazoan divergence.
  • Studying non-metazoan lamins provides a broader evolutionary perspective on nuclear envelope organization.
  • Comparative studies of lamins across diverse eukaryotes can illuminate fundamental biological processes and potential therapeutic targets.