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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...

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...

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...

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...

Role of Ephrin-Eph Signalling in Intestinal Stem Cell Renewal

Role of Ephrin-Eph Signalling in Intestinal Stem Cell Renewal

Erythropoietin-producing hepatocellular carcinoma receptor (Eph) and its ligand, Eph receptor-interacting protein (Ephrin) were first discovered in the human carcinoma cell line, hence the name. Ephrin-Eph interaction guides cells to reach their appropriate location in adult tissues. They also play an essential role in the immune system by helping in immune cell migration, adhesion, and activation. Based on their structure and function, Eph is divided into two classes — EphA and EphB.

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Related Experiment Video

Updated: May 31, 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

Rack1 promotes epithelial cell-cell adhesion by regulating E-cadherin endocytosis.

G Swaminathan¹, C A Cartwright

¹Department of Medicine, Stanford University, Stanford, CA 94305-5187, USA.

|June 21, 2011

Summary

This summary is machine-generated.

Rack1 protein promotes cell-cell adhesion in colon cancer by stabilizing E-cadherin. This reduces cancer cell invasion and metastasis by inhibiting Src kinase activity and E-cadherin endocytosis.

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Last Updated: May 31, 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

An Immunofluorescent Method for Characterization of Barrett’s Esophagus Cells

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Induction and Analysis of Epithelial to Mesenchymal Transition

Induction and Analysis of Epithelial to Mesenchymal Transition

Published on: August 27, 2013

Area of Science:

Cell Biology
Cancer Research
Molecular Biology

Background:

E-cadherin and catenins mediate epithelial cell-cell adhesion, crucial for preventing cancer invasion and metastasis.
Src tyrosine kinase activation disrupts these cell contacts, promoting cancer progression.
Rack1 was previously shown to regulate colon cell growth by suppressing Src activity.

Purpose of the Study:

To investigate Rack1's role in regulating colon cancer cell adhesion and invasion.
To elucidate the molecular mechanisms by which Rack1 influences E-cadherin stability and cell-cell contacts.

Main Methods:

Investigated Rack1's effect on E-cadherin localization and stability.
Assessed the impact of Rack1 on Src-mediated E-cadherin phosphorylation and ubiquitination.
Examined Rack1's role in E-cadherin endocytosis and cell scattering induced by HGF.
Utilized calcium depletion/restoration assays to study cell-cell contact re-assembly.

Main Results:

Rack1 promotes cell-cell adhesion and reduces colon cancer cell invasiveness, partly by inhibiting Src.
Rack1 stabilizes E-cadherin and catenins at cell-cell contacts by preventing Src phosphorylation, Hakai-mediated ubiquitination, and endocytosis.
Rack1 facilitates E-cadherin re-assembly after calcium depletion and blocks HGF-induced E-cadherin endocytosis and cell scatter.

Conclusions:

Rack1 plays a novel role in maintaining intestinal epithelial cell junctional homeostasis.
Rack1 regulates E-cadherin endocytosis, influenced by Src activity and growth factors.
Rack1 represents a potential therapeutic target for reducing colon cancer invasion and metastasis.