Assessment of Splice Variant-Specific Functions of Desmocollin 1 in the Skin

Author:

Cheng Xing12,Mihindukulasuriya Kusal2,Den Zhining2,Kowalczyk Andrew P.3,Calkins Cathárine C.3,Ishiko Akira4,Shimizu Atsushi4,Koch Peter J.12

Affiliation:

1. Departments of Molecular and Cellular Biology

2. Dermatology, Baylor College of Medicine, Houston, Texas

3. Department of Dermatology, Emory University, Atlanta, Georgia

4. Department of Dermatology, Keio University School of Medicine, 35 Shinanomachi, Shinjuku, Tokyo, Japan

Abstract

ABSTRACT Desmocollin 1 (Dsc1) is part of a desmosomal cell adhesion receptor formed in terminally differentiating keratinocytes of stratified epithelia. The dsc1 gene encodes two proteins (Dsc1a and Dsc1b) that differ only with respect to their COOH-terminal cytoplasmic amino acid sequences. On the basis of in vitro experiments, it is thought that the Dsc1a variant is essential for assembly of the desmosomal plaque, a structure that connects desmosomes to the intermediate filament cytoskeleton of epithelial cells. We have generated mice that synthesize a truncated Dsc1 receptor that lacks both the Dsc1a- and Dsc1b-specific COOH-terminal domains. This mutant transmembrane receptor, which does not bind the common desmosomal plaque proteins plakoglobin and plakophilin 1, is integrated into functional desmosomes. Interestingly, our mutant mice did not show the epidermal fragility previously observed in dsc1 -null mice. This suggests that neither the Dsc1a- nor the Dsc1b-specific COOH-terminal cytoplasmic domain is required for establishing and maintaining desmosomal adhesion. However, a comparison of our mutants with dsc1 -null mice suggests that the Dsc1 extracellular domain is necessary to maintain structural integrity of the skin.

Publisher

American Society for Microbiology

Subject

Cell Biology,Molecular Biology

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