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Related Concept Videos

Cadherins in Tissue Organization01:19

Cadherins in Tissue Organization

The cadherins are a superfamily of cell adhesion molecules comprising over 180 variants, with specific tissues expressing a particular combination of cadherin types. Cadherins generally exhibit homophilic binding; i.e., cadherins on one cell bind to cadherins of the same or closely related type on another cell. Thus, cells of the same type have a specific affinity to bind to each other and sort themselves into clusters to form tissues.
Cell Sorting During Development
Cell sorting plays an...
Structure of Cadherins01:25

Structure of Cadherins

The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This diversity of cadherins...
Adherens Junctions01:24

Adherens Junctions

Strong contact points between adjacent cells anchor them to each other, forming tissues. Such anchoring junctions are of two types –  adherens junctions and desmosomes. Adherens junctions are abundant in tissues such as  epithelium and endothelium, forming a continuous zone of adhesion called the adhesion belt. In other tissues, such as  heart muscle, they appear as clusters, linking the cells to produce coordinated heart muscle contraction.
Adherens Junctions are Dynamic
The endothelial cells...
Tension Response at Adherens Junctions01:26

Tension Response at Adherens Junctions

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.
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin homology) domains...
Catenins01:23

Catenins

Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the adherens...
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

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.
Some...

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Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules
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Published on: October 17, 2014

Intestinal LI-cadherin acts as a Ca2+-dependent adhesion switch.

Markus W Wendeler1, Detlev Drenckhahn, Reinhard Gessner

  • 1Biomedical Research Center, Virchow Hospital of Charité Medical School Berlin, D-13353 Berlin, Germany.

Journal of Molecular Biology
|May 22, 2007
PubMed
Summary

LI-cadherin, a protein in the intestinal epithelium, mediates cell adhesion with low affinity. Its binding is highly sensitive to calcium levels, potentially acting as a calcium-regulated switch.

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Area of Science:

  • Cell Biology
  • Biophysics
  • Biochemistry

Background:

  • Cadherins are calcium-dependent glycoproteins crucial for cell-cell adhesion and epithelial integrity.
  • LI-cadherin and E-cadherin are key cadherins in the intestinal epithelium, differing in structure and localization.
  • LI-cadherin lacks catenin interaction and is evenly distributed, unlike E-cadherin concentrated in adherens junctions.

Purpose of the Study:

  • To investigate the unique homotypic adhesion mechanism of LI-cadherin.
  • To analyze LI-cadherin's binding parameters at single-molecule and cellular levels.
  • To understand LI-cadherin's role in the intestinal epithelial adhesive system.

Main Methods:

  • Atomic force microscopy
  • Affinity chromatography
  • Laser tweezer experiments

Main Results:

  • LI-cadherin exhibits low-affinity homotypic trans-interaction with a short binding lifetime (1.4 s).
  • LI-cadherin binding shows high cooperativity in response to extracellular calcium concentrations below physiological levels.
  • LI-cadherin's adhesive properties differ significantly from E-cadherin.

Conclusions:

  • LI-cadherin may function as a calcium-regulated switch for adhesion on basolateral membranes of intestinal epithelial cells.
  • The distinct binding characteristics of LI-cadherin are linked to its unique structural properties.
  • LI-cadherin plays a specialized role in regulating cell-cell adhesion within the intestinal epithelium.