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Related Concept Videos

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...
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...
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...
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...
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...

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Related Experiment Video

Updated: Jun 21, 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

Characterizing the initial encounter complex in cadherin adhesion.

Sanjeevi Sivasankar1, Yunxiang Zhang, W James Nelson

  • 1Department of Physics and Astronomy, Iowa State University, Ames, IA 50011, USA. sivasank@iastate.edu

Structure (London, England : 1993)
|August 4, 2009
PubMed
Summary
This summary is machine-generated.

Cadherins initially form weak, non-swapped complexes before adopting a strong, strand-swapped dimer structure. This suggests cadherin dimerization involves an induced fit mechanism for cell adhesion.

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

Adhesion Frequency Assay for In Situ Kinetics Analysis of Cross-Junctional Molecular Interactions at the Cell-Cell Interface
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Adhesion Frequency Assay for In Situ Kinetics Analysis of Cross-Junctional Molecular Interactions at the Cell-Cell Interface

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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
  • Biophysics
  • Cell Adhesion Mechanisms

Background:

  • Cadherins are calcium-dependent cell-cell adhesion proteins crucial for tissue integrity.
  • Adhesion involves a 'strand swapping' mechanism between extracellular domains (EC1) of opposing cadherins.
  • The precise mechanism of cadherin strand-swapped dimer formation remains unclear.

Purpose of the Study:

  • To elucidate the initial steps and mechanism of cadherin dimerization.
  • To investigate the role of the tryptophan-2 residue in early cadherin interactions.
  • To characterize the properties of the initial cadherin encounter complex.

Main Methods:

  • Single-molecule fluorescence resonance energy transfer (smFRET) was employed.
  • Single-molecule force measurements using atomic force microscopy (AFM) were performed.
  • These techniques allowed for the study of cadherin interactions at the single-molecule level.

Main Results:

  • Cadherins form an initial, weak, calcium-dependent encounter complex via EC1 domains.
  • This initial complex does not involve tryptophan-2 swapping and has 25% of the final dimer's bond strength.
  • The findings indicate a distinct intermediate state preceding stable dimerization.

Conclusions:

  • Cadherin dimerization likely proceeds through an induced fit mechanism.
  • Monomers first form a tryptophan-2 independent encounter complex.
  • Subsequent conformational changes lead to the formation of the stable, strand-swapped dimer.