ArticleThe Journal of biological chemistry2011
Membrane-impermeable cross-linking provides evidence for homophilic, isoform-specific binding of desmosomal cadherins in epithelial cells.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 67 citations in OpenAlex.
- Structural Insights into Ordered Multicomponent Assemblies in Cell Junctions.Advances in experimental medicine and biology · 2026Review
- The transmembrane domain of the desmosomal cadherin desmoglein-1 governs lipid raft association to promote desmosome adhesive strength.Molecular biology of the cell · 2024Article
- Desmosomes at a glance.Journal of cell science · 2024Review
- The intercalated disc: a unique organelle for electromechanical synchrony in cardiomyocytes.Physiological reviews · 2023Review
- Significance of anti-desmocollin autoantibodies in pemphigus.The Journal of dermatology · 2023Review
- Desmoglein 2 can undergo CaBiophysical journal · 2022Article
- Bidirectional regulation of desmosome hyperadhesion by keratin isotypes and desmosomal components.Cellular and molecular life sciences : CMLS · 2022Article
- DNA Methylation Mediates EMT Gene Expression in Human Pancreatic Ductal Adenocarcinoma Cell Lines.International journal of molecular sciences · 2022Article
- Mechanisms Causing Acantholysis in Pemphigus-Lessons from Human Skin.Frontiers in immunology · 2022Review
- Regulation of intestinal epithelial intercellular adhesion and barrier function by desmosomal cadherin desmocollin-2.Molecular biology of the cell · 2021Article
- Autoantibody-Specific Signalling in Pemphigus.Frontiers in medicine · 2021Review
- Identification of Docetaxel as a Potential Drug to Promote HDL Biogenesis.Frontiers in pharmacology · 2021Article
- Desmosomal Hyperadhesion Is Accompanied with Enhanced Binding Strength of Desmoglein 3 Molecules.Biophysical journal · 2020Article
- The desmosome as a model for lipid raft driven membrane domain organization.Biochimica et biophysica acta. Biomembranes · 2020Review
- Dsg2 Upregulation as a Rescue Mechanism in Pemphigus.Frontiers in immunology · 2020Article
- Plakophilin 1 but not plakophilin 3 regulates desmoglein clustering.Cellular and molecular life sciences : CMLS · 2019Article
- Desmoglein 2, but not desmocollin 2, protects intestinal epithelia from injury.Mucosal immunology · 2018Article
- Pathogenic IgG4 autoantibodies from endemic pemphigus foliaceus recognize a desmoglein-1 conformational epitope.Journal of autoimmunity · 2018Article
- Keratins Regulate p38MAPK-Dependent Desmoglein Binding Properties in Pemphigus.Frontiers in immunology · 2018Article
- Pemphigus-A Disease of Desmosome Dysfunction Caused by Multiple Mechanisms.Frontiers in immunology · 2018Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
Abstract
Desmosomes and adherens junctions are cadherin-based protein complexes responsible for cell-cell adhesion of epithelial cells. Type 1 cadherins of adherens junctions show specific homophilic adhesion that plays a major role in developmental tissue segregation. The desmosomal cadherins, desmocollin and desmoglein, occur as several different isoforms with overlapping expression in some tissues where different isoforms are located in the same desmosomes. Although adhesive binding of desmosomal cadherins has been investigated in a variety of ways, their interaction in desmosome-forming epithelial cells has not been studied. Here, using extracellular homobifunctional cross-linking, we provide evidence for homophilic and isoform-specific binding between the Dsc2, Dsc3, Dsg2, and Dsg3 isoforms in HaCaT keratinocytes and show that it represents trans interaction. Furthermore, the cross-linked adducts are present in the detergent-insoluble fraction, and electron microscopy shows that extracellular cross-linking probably occurs in desmosomes. We found no evidence for either heterophilic or cis interaction, but neither can be completely excluded by our data. Mutation of amino acid residues Trp-2 and Ala-80 that are important for trans interaction in classical cadherin adhesive binding abolished Dsc2 binding, indicating that these residues are also involved in desmosomal adhesion. These interactions of desmosomal cadherins may be of key importance for their ordered arrangement within desmosomes that we believe is essential for desmosomal adhesive strength and the maintenance of tissue integrity.
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