Desmoglein-1, differentiation, and disease
- PMID: 23524961
- PMCID: PMC3613937
- DOI: 10.1172/JCI69071
Desmoglein-1, differentiation, and disease
Abstract
Desmoglein-1 (DSG1), a desmosomal protein, maintains the structure of epidermis through its adhesive function. However, heterozygous mutations in DSG1 in humans result in abnormal differentiation, as does downregulation of DSG1 in human skin organ culture, suggesting that it may have important signaling functions. In this issue of the JCI, Harmon et al. elucidate how the binding of the DSG1 cytoplasmic tail to the scaffolding protein Erbin decreases signaling through the Ras-Raf pathway to promote stratification and differentiation of keratinocytes in the epidermis.
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Comment on
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Desmoglein-1/Erbin interaction suppresses ERK activation to support epidermal differentiation.J Clin Invest. 2013 Apr;123(4):1556-70. doi: 10.1172/JCI65220. Epub 2013 Mar 25. J Clin Invest. 2013. PMID: 23524970 Free PMC article.
References
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- Steinberg MS, Shida H, Giudice GJ, Shida M, Patel NH, Blaschuk OW. On the molecular organization, diversity and functions of desmosomal proteins. Ciba Found Symp. 1987;125:3–25. - PubMed
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- Bornslaeger EA, et al. Plakophilin 1 interferes with plakoglobin binding to desmoplakin, yet together with plakoglobin promotes clustering of desmosomal plaque complexes at cell-cell borders. J Cell Sci. 2001;114(pt 4):727–738. - PubMed
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