Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Structure of Cadherins

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 Junctions

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...

Cadherins in Tissue Organization

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...

Catenins

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 Junctions

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...

Anchoring Junctions

Anchoring Junctions

Anchoring junctions are multiprotein complexes that help cells connect to other cells and the extracellular matrix. Anchoring junctions are present on the lateral and basal surfaces of cells, providing strong and flexible connections. Focal adhesions are often formed due to cell interactions with the ECM substrata, which initiate signal transduction via kinase cascades and other mechanisms. Together, they provide stability and tissue integrity. There are three types of anchoring junctions:...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

[Elucidation of the Mechanisms of RNA Diseases and Manipulation of RNA].

Yakugaku zasshi : Journal of the Pharmaceutical Society of Japan·2025

Same author

[Elucidation of the Molecular Mechanism Underlying Aberrant Formation of RNA Granules in Neurons of ALS Patients and Its Regulation].

Yakugaku zasshi : Journal of the Pharmaceutical Society of Japan·2025

Same author

dCas13-mediated translational repression for accurate gene silencing in mammalian cells.

Nature communications·2024

Same author

Strengthening E-cadherin adhesion via antibody-mediated binding stabilization.

Structure (London, England : 1993)·2023

Same author

The Plasma Membrane Polarity Is Higher in the Neuronal Growth Cone than in the Cell Body of Hippocampal and Cerebellar Granule Neurons.

Biological & pharmaceutical bulletin·2023

Same author

Strengthening E-cadherin adhesion via antibody mediated binding stabilization.

bioRxiv : the preprint server for biology·2023

Search research articles

Related Experiment Video

Updated: Jul 16, 2026

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules

Published on: October 17, 2014

Cadherin conformations associated with dimerization and adhesion.

Hitomi Tsuiji¹, Liang Xu, Kathleen Schwartz

¹Department of Cell Biology, University of Virginia School of Medicine, Charlottesville, Virginia 22903, USA.

The Journal of Biological Chemistry

|March 10, 2007

Summary

Monoclonal antibodies reveal C-cadherin

Area of Science:

Cell Adhesion Biology
Protein Conformation Studies
Immunology

Background:

Cadherins are crucial cell adhesion molecules involved in tissue development and homeostasis.
Understanding C-cadherin conformation is key to elucidating its functional regulation.

Purpose of the Study:

To generate and characterize monoclonal antibodies (mAbs) targeting specific C-cadherin conformations.
To investigate the relationship between C-cadherin conformation, dimerization, and cell adhesion activity.

Main Methods:

Generation of conformation-specific monoclonal antibodies against C-cadherin.
Epitope mapping of mAbs to different C-cadherin ectodomain regions (EC1-EC5).
Analysis of mAb binding to wild-type and mutant C-cadherin in monomeric and dimeric forms, and on cell surfaces.

More Related Videos

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

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

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

Published on: November 2, 2011

Related Experiment Videos

Last Updated: Jul 16, 2026

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules

Bead Aggregation Assays for the Characterization of Putative Cell Adhesion Molecules

Published on: October 17, 2014

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

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

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

Published on: November 2, 2011

Main Results:

mAbs recognizing different C-cadherin epitopes (EC1, EC1-EC2 interface, EC4, EC5) were generated.
A W2A mutant, when dimerized, regained partial homophilic binding but not full adhesion.
No mAbs distinguished physiological states of C-cadherin on cell surfaces, indicating dimerization changes are not the primary regulatory mechanism.

Conclusions:

C-cadherin's cell adhesion activity is not regulated by simple changes in dimerization.
The EC3-EC5 domains are less accessible on the cell surface, suggesting involvement in cadherin organization.
C-cadherin organization and dimerization likely involve the EC2-EC5 domains.