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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...
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...
Cell Adhesion Molecules - Types and Functions01:20

Cell Adhesion Molecules - Types and Functions

Cell adhesion molecules (CAMs) are pivotal to multicellularity and the coordinated functioning of tissues and organ systems. They enable physical interactions between cells and provide mechanical strength to tissues. They also function as receptors for signal transmission across the plasma membrane. The CAMs are broadly classified into four families - integrins, cadherins, selectins, and immunoglobulin-like CAMs (IgCAMs).
CAM Families
The Integrin family of proteins is primarily  involved in a...

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Related Experiment Video

Updated: May 22, 2026

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules
08:15

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules

Published on: October 17, 2014

Thinking outside the cell: how cadherins drive adhesion.

Julia Brasch1, Oliver J Harrison, Barry Honig

  • 1Department of Biochemistry and Molecular Biophysics, Columbia University, 1150 Saint Nicholas Avenue, New York, NY 10032, USA.

Trends in Cell Biology
|May 5, 2012
PubMed
Summary

Cadherins are cell adhesion proteins. Classical cadherins form adhesive dimers via a two-step process, promoting cell junction assembly by reducing flexibility.

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Last Updated: May 22, 2026

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules
08:15

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Published on: October 17, 2014

Ligand Nano-cluster Arrays in a Supported Lipid Bilayer
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Analyzing Cell Surface Adhesion Remodeling in Response to Mechanical Tension Using Magnetic Beads
07:55

Analyzing Cell Surface Adhesion Remodeling in Response to Mechanical Tension Using Magnetic Beads

Published on: March 8, 2017

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Cadherins are cell surface glycoproteins mediating cell-cell adhesion.
  • They possess extracellular cadherin (EC) domains with beta-sandwich folds, similar to immunoglobulin domains.
  • Classical cadherins are well-characterized, utilizing trans homodimerization for adhesion and cis clustering for adherens junction assembly.

Purpose of the Study:

  • To elucidate the molecular mechanisms of cadherin-mediated cell adhesion.
  • To understand the structural basis of trans adhesive dimer formation in classical cadherins.
  • To investigate the role of dimer flexibility in adherens junction assembly.

Main Methods:

  • Structural analysis of cadherin ectodomains.
  • Biophysical techniques to study protein-protein interactions.
  • Cell-based assays to observe junction formation.

Main Results:

  • Cadherin trans dimers form through a two-step process involving an 'X-dimer' intermediate.
  • Mature trans dimers adopt a 'strand-swapped' conformation.
  • Reduced flexibility of trans dimers facilitates adherens junction assembly by lowering the entropic cost of cis oligomerization.

Conclusions:

  • The formation of less flexible trans dimers is crucial for efficient cadherin-mediated cell adhesion and adherens junction assembly.
  • Classical cadherins employ a specific dimerization mechanism to regulate cell-cell contact.
  • Non-classical cadherins may utilize alternative adhesive strategies.