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Related Concept Videos

Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

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Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
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The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
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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.
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Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
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Related Experiment Video

Updated: Oct 3, 2025

Labeling F-actin Barbed Ends with Rhodamine-actin in Permeabilized Neuronal Growth Cones
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The Discovery and Function of Filaggrin.

J Kenneth Hoober1, Laura L Eggink1

  • 1Susavion Biosciences, Inc., 1615 W University Drive, Suite 132, Tempe, AZ 85281, USA.

International Journal of Molecular Sciences
|February 15, 2022
PubMed
Summary

Filaggrin, a key protein in the skin's outer layer, aggregates keratin and aids in forming an impermeable barrier. Loss-of-function mutations in its gene cause diseases like ichthyosis vulgaris and atopic dermatitis.

Keywords:
atopic dermatitiscorneodesmosomeseczemafilaggrinhistidine-rich proteinichthyosis vulgariskeratohyalin granulesloss-of-function mutationsprofilaggrintransglutaminase

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Area of Science:

  • Dermatology
  • Biochemistry
  • Genetics

Background:

  • Keratohyalin granules in epidermal cells were identified in the mid-19th century.
  • Early research in the 1960s indicated a high histidine content in these granules.
  • Filaggrin, a histidine-rich protein, was discovered for its role in keratin aggregation.

Purpose of the Study:

  • To elucidate the historical research and discovery of filaggrin.
  • To understand the function of filaggrin in epidermal differentiation and barrier formation.
  • To investigate the genetic basis of filaggrin-related skin disorders.

Main Methods:

  • Histochemical staining for histidine.
  • Radioautography to track protein synthesis.
  • Gene sequencing to identify mutations.

Main Results:

  • Filaggrin facilitates corneocyte collapse into an impermeable skin barrier.
  • Profilaggrin gene mutations lead to filaggrin absence and barrier dysfunction.
  • Loss-of-function mutations in the profilaggrin gene cause ichthyosis vulgaris and atopic dermatitis.

Conclusions:

  • Filaggrin is crucial for epidermal barrier integrity and skin hydration.
  • Genetic defects in filaggrin production result in significant skin barrier diseases.
  • Understanding filaggrin's role highlights the complexity of maintaining a healthy epidermis.