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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...
Desmosomes01:05

Desmosomes

The term desmosome derives from the Greek words "desmo" and "soma" meaning "adhesion bodies." This structure was first observed during the late 1800s and described as small, dense nodules in the epidermis. Desmosomes are button-like structures that help form an interlinked network of intermediate filaments across the cells. These junctions are  essential to hold cells together under mechanical stress and to maintain tissue integrity. Desmosomes are multi-protein complexes comprising desmosomal...

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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

Two-step adhesive binding by classical cadherins.

Oliver J Harrison1, Fabiana Bahna, Phini S Katsamba

  • 1Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York, USA.

Nature Structural & Molecular Biology
|March 2, 2010
PubMed
Summary
This summary is machine-generated.

Cadherin X dimers, initially thought distinct, are actually intermediates. Mutants show X dimers form first, then strand-swapped dimers, clarifying cadherin homophilic binding mechanisms.

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Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules
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Area of Science:

  • Molecular biology
  • Structural biology
  • Biochemistry

Background:

  • Classical cadherins form dimers through various configurations, including N-terminal beta-strand swapping and X dimers.
  • Previous structural studies presented conflicting models for cadherin dimerization.

Purpose of the Study:

  • To investigate the relationship between strand-swapped and X dimer configurations in classical cadherins.
  • To elucidate the role of X dimers in cadherin homophilic binding.

Main Methods:

  • Generation of strand-swapping mutants for type I and II classical cadherins.
  • Surface plasmon resonance (SPR) assays to measure binding kinetics (short- and long-time frames).
  • Analysis of cadherin dimer formation and exchange rates.

Main Results:

  • Strand-swapping cadherin mutants form X dimers.
  • Mutants impaired in X-dimer formation exhibit delayed homophilic binding, with affinities similar to wild-type in long-time frame assays.
  • These mutants show slower monomer-dimer exchange rates.

Conclusions:

  • X dimers represent binding intermediates in classical cadherin homophilic binding.
  • The formation of X dimers precedes and facilitates the formation of strand-swapped dimers.
  • These findings reconcile disparate structural observations and provide a unified model for cadherin dimerization.