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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...
Basal Lamina are the Specialized Form of ECM01:03

Basal Lamina are the Specialized Form of ECM

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.
Proteins...
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...
Mechanism of Lamellipodia Formation01:31

Mechanism of Lamellipodia Formation

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...
Structural Protein Function01:56

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to form...
Structural Protein Function01:56

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to form...

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Updated: May 10, 2026

Generating a Fractal Microstructure of Laminin-111 to Signal to Cells
06:56

Generating a Fractal Microstructure of Laminin-111 to Signal to Cells

Published on: September 28, 2020

From lamins to lamina: a structural perspective.

Monika Zwerger1, Ohad Medalia

  • 1Department of Biochemistry, University of Zurich, Winterthurerstrasse 190, 8057, Zurich, Switzerland.

Histochemistry and Cell Biology
|June 8, 2013
PubMed
Summary
This summary is machine-generated.

Nuclear lamins provide structural support and regulate nuclear processes. Mutations in lamins cause laminopathies, a group of diseases affecting various tissues, with their molecular basis still under investigation.

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Last Updated: May 10, 2026

Generating a Fractal Microstructure of Laminin-111 to Signal to Cells
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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • Lamins are key components of the nuclear lamina, essential for nuclear structure and function.
  • Lamins and associated proteins are implicated in DNA replication, gene regulation, and signaling.
  • Mutations in lamin A and related proteins lead to diverse diseases known as laminopathies.

Purpose of the Study:

  • To review the structural aspects of lamins and nuclear lamina organization.
  • To explore the molecular basis of laminopathies and tissue-specific effects.
  • To provide a comprehensive view on lamin organization in health and disease.

Main Methods:

  • Review of recent scientific literature on lamin structure and function.
  • Analysis of studies investigating lamin mutations and associated diseases.
  • Discussion of molecular and structural data related to nuclear lamina organization.

Main Results:

  • The nuclear lamina provides crucial structural support to the nucleus.
  • Lamin mutations are linked to a spectrum of diseases, including muscular dystrophies and premature aging.
  • The precise molecular organization and disease mechanisms of lamins remain incompletely understood.

Conclusions:

  • Understanding lamin structure is vital for deciphering laminopathies.
  • Further research is needed to elucidate the complex relationship between lamin organization and disease pathogenesis.
  • Targeting nuclear lamina structure may offer therapeutic avenues for laminopathies.