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Related Concept Videos

Cell-matrix's Response to Mechanical Forces01:13

Cell-matrix's Response to Mechanical Forces

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In animal cells, the extracellular matrix allows cells within tissues to withstand external stresses and transmits signals from the outside of the cell to the inside. The extracellular matrix is extensive, and its composition varies between different types of tissues. For example, the reticular fibers and ground substance make up the ECM in loose connective tissue, while collagen and bone minerals make up the ECM of bone tissue. 
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The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
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Actin and myosin or actomyosin filaments also play a significant role in cells other than those involved in muscle contraction (which occurs within the sarcomere of muscle cells). The mechanism of non-muscle cell contractile bundles was first observed in Dictyostelium and Acanthamoeba. In non-muscle cells, two bundles are commonly found: stress fibers and actomyosin adherence belts. These contractile bundles are smaller and less organized than the ones found in muscle cells. They  are held...
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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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Actin crosslinking is required for force sensing at tricellular junctions.

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Summary

Fimbrin protein stabilizes epithelial cell adhesion under mechanical stress by reinforcing actin networks. Its absence disrupts force-response pathways, compromising tissue integrity during remodeling.

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Area of Science:

  • Cell Biology
  • Biophysics
  • Developmental Biology

Background:

  • Mechanical forces are crucial for tissue development (morphogenesis).
  • Epithelial adherens junctions manage these forces via actin cytoskeleton connections.
  • The in vivo response of junctional actin networks to force remains unclear.

Purpose of the Study:

  • To investigate the role of the actin crosslinker Fimbrin in epithelial force response.
  • To understand how Fimbrin influences actomyosin contractility and cell adhesion under tension.

Main Methods:

  • In vivo studies of epithelial tissues under mechanical tension.
  • Analysis of Fimbrin recruitment to tricellular junctions.
  • Assessment of actomyosin contractility and myosin-II activity.
  • Evaluation of junction-stabilizing protein recruitment.

Main Results:

  • Fimbrin is recruited to tricellular junctions under tension.
  • Fimbrin amplifies actomyosin contractility and stabilizes cell adhesion.
  • Loss of Fimbrin impairs actin reorganization and myosin-II activity under force.
  • Fimbrin deficiency disrupts the recruitment of junction-stabilizing proteins, leading to adhesion failure.
  • Increased Fimbrin activity aberrantly stabilizes adhesion by activating force-response pathways.

Conclusions:

  • Fimbrin-mediated actin crosslinking is vital for modulating actomyosin dynamics during epithelial remodeling.
  • Fimbrin reinforces cell adhesion under mechanical tension.
  • Fimbrin acts as a key regulator of force-response pathways in epithelial tissues.