Adherens junction

From Wikipedia, the free encyclopedia

Principal interactions of structural proteins at cadherin-based adherens junction. Actin filaments are associated with adherens junctions in addition to several other actin-binding proteins such as vinculin. The head domain of vinculin associates to E-cadherin via α-, β - and γ -catenins. The tail domain of vinculin binds to membrane lipids and to actin filaments.
Principal interactions of structural proteins at cadherin-based adherens junction. Actin filaments are associated with adherens junctions in addition to several other actin-binding proteins such as vinculin. The head domain of vinculin associates to E-cadherin via α-, β - and γ -catenins. The tail domain of vinculin binds to membrane lipids and to actin filaments.

Adherens junctions (or zonula adherens) are protein complexes that occur at cell-cell junctions in epithelial tissues, usually more basal than tight junctions.

They can appear as bands encircling the cell (zonula adherens) or as spots of attachment to the extracellular matrix (adhesion plaques).

A similar cell junction in non-epithelial cells is the fascia adherens. It is structurally the same, but appears in ribbon like patterns that do not completely encircle the cells. One example is in cardiomyocytes.

Contents

[edit] Proteins

They are composed of three major proteins:

  • cadherins. The cadherins are a family of transmembrane proteins that form homodimers in a calcium-dependent manner with other cadherin molecules on adjacent cells.
  • β-catenin and α-catenin. The catenins both form a complex with the intracellular portion of the cadherin molecule.

[edit] Models

Adherens junctions were, for many years, thought to share the characteristic of anchor cells through their cytoplasmic actin filaments.

The accepted model has been that adherens junctions serve as a bridge connecting the actin cytoskeleton of neighboring cells through direct interaction. However, scientists have not been able to isolate the quaternary complex of cadherin-βcatenin-αcatenin-actin in vitro. Recent data (2005) from 2 labs at Stanford University published in the journal Cell demonstrates that membrane associated actin is several fold less stable compared to components of the adherens junctional complex.[1][2]

Additionally, the authors found that monomeric α-catenin preferentially binds to the cadherin junction complex through β-catenin. Dimeric α-catenin preferentially binds to actin and suppresses Arp2/3 complex-mediated actin branching, thus acting as a molecular switch to regulate actin polymerization.

Adherens junctions may serve as a regulatory module to maintain the actin contractile ring with which it is associated in microscopic studies.

[edit] References

  1. ^ Yamada S, Pokutta S, Drees F, Weis W, Nelson W (2005). "Deconstructing the cadherin-catenin-actin complex.". Cell 123 (5): 889–901. doi:10.1016/j.cell.2005.09.020. PMID 16325582. 
  2. ^ Drees F, Pokutta S, Yamada S, Nelson W, Weis W (2005). "Alpha-catenin is a molecular switch that binds E-cadherin-beta-catenin and regulates actin-filament assembly.". Cell 123 (5): 903–15. doi:10.1016/j.cell.2005.09.021. PMID 16325583. 

[edit] External links

v • d • e
Histology: epithelial tissue
Types
Features
 This cell biology article is a stub. You can help Wikipedia by expanding it.