Desmoplakins (DP) I and II and the 230 kDa bullous pemphigoid antigen (BPA) are major plaque components of the desmosome and hemidesmosome, respectively. In the cell, these adhesion structures are both linked with the intermediate filament (IF) cytoskeleton. Comparisons of DP I and II with BPA sequences have indicated that these molecules are likely to form extended dumbbell-shaped dimers with flexible central rod and globular end domains. Later comparisons of DP and BPA amino acid sequences with that of plectin (PL), a 466 kDa IF-linked protein, also revealed large scale homology. In the C-terminal ends, which contain a 38-residue repeating motif, identities imply that DP and PL are closer relatives However, among their N-terminal ends, BPA is more closely related to PL Other common features of the three proteins are the presence of an extensive heptad repeat substructure in their central and N-domains, similar periodic distributions of charged residues in the C-domains, and the formation of two-stranded alphahelical coiled-coils in the central rods All these observations suggest that DP I and II, BPA and PL belong to a gene family encoding proteins involved in IF organization.
|Original language||English (US)|
|State||Published - Dec 1 1997|
ASJC Scopus subject areas
- Molecular Biology