Related Experiment Video
Updated: May 30, 2026

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro
Published on: January 11, 2017
A role for caveolin-1 in desmoglein binding and desmosome dynamics
D Brennan1, S Peltonen, A Dowling
1Department of Dermatology and Cutaneous Biology, Thomas Jefferson University, Philadelphia, PA 19107, USA.
Desmoglein-2 (Dsg2) protein interacts with caveolin-1 (Cav-1), impacting cell adhesion and signaling in skin carcinomas. This interaction and Dsg2 processing may drive tumor progression and malignant transformation.
Area of Science:
- Cell Biology
- Molecular Oncology
- Dermatology
Background:
- Desmoglein-2 (Dsg2) is a desmosomal cadherin implicated in human skin carcinomas.
- Dsg2's role in intercellular adhesion and mitogenic signaling in cancer is not fully understood.
- The mechanisms linking Dsg2 to cancer progression require further elucidation.
Purpose of the Study:
- To investigate the association between Desmoglein-2 (Dsg2) and caveolin-1 (Cav-1).
- To explore the functional consequences of Dsg2-Cav-1 interaction and Dsg2 processing in cancer.
- To understand Dsg2's contribution to malignant transformation.
Main Methods:
- Sequence analysis to identify Dsg2's Cav-1-binding motif.
- In vitro experiments using competing peptides to disrupt Dsg2-Cav-1 interaction.
- Analysis of Dsg2 proteolytic processing and localization in lipid rafts.
- In vivo studies in transgenic mice with Dsg2-overexpressing skin tumors.
Main Results:
- Dsg2 associates with caveolin-1 (Cav-1), a key component of caveolae.
- A Dsg2-Cav-1 interaction motif was identified, and its disruption affected epithelial integrity.
- Dsg2 undergoes proteolytic processing, generating shed ectodomains and membrane-spanning fragments.
- Dsg2 fragments and full-length Dsg2 localize to lipid rafts, and their accumulation disrupts cell adhesion.
- Elevated Dsg2 proteolytic products were observed in skin tumors of Dsg2-overexpressing mice.
Conclusions:
- Dsg2-Cav-1 association may regulate signaling pathways and cell-surface adhesion molecule presentation.
- Accumulation of truncated Dsg2 interferes with desmosome assembly and cell-cell adhesion.
- These Dsg2-mediated mechanisms contribute to malignant transformation and skin carcinoma progression.
More Related Videos
12:15The C. elegans Intestine As a Model for Intercellular Lumen Morphogenesis and In Vivo Polarized Membrane Biogenesis at the Single-cell Level: Labeling by Antibody Staining, RNAi Loss-of-function Analysis and Imaging
Published on: October 3, 2017
10:19In Vitro Reconstitution of the Actin Cytoskeleton Inside Giant Unilamellar Vesicles
Published on: August 25, 2022
Related Concept Videos
Desmosomes
Pinching-off of Coated Vesicles
Assembly of Signaling Complexes
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Catenins
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...
Structure of Cadherins
Mechanisms of Membrane Domain Formation
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...