DSC1

DSC1 is the gene that encodes desmocollin-1, a member of the desmosomal cadherin family. Desmocollin-1 is a calcium‑dependent cell adhesion protein located in desmosomes, specialized intercellular junctions that provide mechanical integrity to tissues subjected to shear, particularly stratified epithelia such as the epidermis and oral mucosa.

The DSC1 protein participates in desmosomal adhesion by forming trans interactions with desmogleins and by linking to the desmosomal plaque through plakophilins and desmoplakin, thereby anchoring to the intermediate filament cytoskeleton. Its structure includes extracellular cadherin repeats, a single transmembrane domain, and a cytoplasmic tail that mediates protein–protein interactions necessary for junction assembly and stability.

DSC1 expression is prominent in stratified epithelia and its desmosomal localization contributes to the cohesion of keratinocytes. Isoforms may arise from alternative splicing, reflecting tissue- or development-specific regulation of the desmosomal adhesive complex.

Genetics and disease associations for DSC1 are primarily linked to rare disorders affecting epithelial barrier function. Mutations or dysregulation of DSC1 have been implicated in skin fragility and ectodermal dysplasia-like phenotypes in humans. Alterations in desmosomal components, including DSC1, are also studied for their potential roles in cancer progression, given changes in cell–cell adhesion that accompany tumor biology.

Interactions within the desmosomal network include desmogleins (DSG1–DSG3), other desmosomal cadherins such as DSC2 and DSC3, plakophilins (PKP1–PKP3), and desmoplakin (DSP). Research in human tissues and animal models continues to define DSC1’s contributions to junction assembly, barrier function, and tissue mechanics.