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

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...

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:...

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...

Intracellular Signaling Affects Focal Adhesions

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...

Desmosomes

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...

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...

You might also read

Related Articles

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

Sort by

Same author

Association of preoperative neoplasia and rectal cuff inflammation on initial pouchoscopy with subsequent neoplasia development in inflammatory bowel disease patients with an ileal pouch-anal anastomosis: a case-control study.

Inflammatory bowel diseases·2026

Same author

The protein tyrosine phosphatase CD45 promotes PMN transepithelial migration, antimicrobial function and colonic mucosal repair.

JCI insight·2026

Same author

RUNX2 promotes chromatin accessibility and WNT signaling in inflamed intestinal epithelial cells.

Mucosal immunology·2026

Same author

Targeting Fatty Acid Synthase With Berberine Promotes IL-10 Production in Macrophages and Prevents Relapse in a Murine Colitis Model.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology·2026

Same author

The Protein Tyrosine Phosphatase CD45 promotes PMN Transepithelial Migration, Antimicrobial Function and Colonic Mucosal Repair.

bioRxiv : the preprint server for biology·2026

Same author

Advancing drug discovery for inflammatory bowel diseases through human intestinal organoid-based models.

Expert opinion on drug discovery·2026

Search research articles

Related Experiment Video

Updated: Jul 7, 2026

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes

Published on: June 13, 2014

Cis-dimerization mediates function of junctional adhesion molecule A.

Eric A Severson¹, Liangyong Jiang, Andrei I Ivanov

¹Epithelial Pathobiology Research Unit, Department of Pathology, Emory University, Atlanta, GA 30322, USA.

Molecular Biology of the Cell

|February 15, 2008

Summary

This summary is machine-generated.

Junctional adhesion molecule-A (JAM-A) dimerization is crucial for epithelial cell migration and adhesion. Disrupting JAM-A dimerization reduces beta1 integrin levels, impacting cell movement.

More Related Videos

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

Analysis of Protein-protein Interactions and Co-localization Between Components of Gap, Tight, and Adherens Junctions in Murine Mammary Glands

Analysis of Protein-protein Interactions and Co-localization Between Components of Gap, Tight, and Adherens Junctions in Murine Mammary Glands

Published on: May 30, 2017

Related Experiment Videos

Last Updated: Jul 7, 2026

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes

Published on: June 13, 2014

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

Analysis of Protein-protein Interactions and Co-localization Between Components of Gap, Tight, and Adherens Junctions in Murine Mammary Glands

Analysis of Protein-protein Interactions and Co-localization Between Components of Gap, Tight, and Adherens Junctions in Murine Mammary Glands

Published on: May 30, 2017

Area of Science:

Cell Biology
Molecular Biology
Biochemistry

Background:

Junctional adhesion molecule-A (JAM-A) is a tight junction protein involved in cell adhesion and migration.
The functional significance of JAM-A cis-homodimerization remains unclear, despite structural evidence.

Purpose of the Study:

To investigate the role of JAM-A cis-dimerization in regulating epithelial cell migration and adhesion.
To elucidate the molecular mechanisms by which JAM-A dimerization affects cell behavior.

Main Methods:

Overexpression of dimerization-defective JAM-A mutants in 293T cells.
Use of dimerization-blocking antibodies.
Analysis of beta1 integrin protein and mRNA levels.
Assessment of beta1 integrin localization and degradation.
Overexpression of beta1 integrin to restore cell migration.

Main Results:

Dimerization-defective JAM-A mutants inhibited cell spreading and migration.
Disruption of JAM-A dimerization led to diminished beta1 integrin protein levels, not mRNA.
Internalization and subsequent degradation of beta1 integrin were observed.
Overexpression of beta1 integrin rescued the migratory defect in JAM-A dimerization-defective cells.
The PDZ-binding motif of JAM-A is essential for its functional effects on dimerization.

Conclusions:

JAM-A dimerization regulates epithelial cell migration and adhesion.
This regulation occurs through posttranscriptional control of beta1 integrin levels.
The carboxy-terminal PDZ-binding motif is critical for JAM-A's function in dimerization-dependent cell regulation.