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© The Rockefeller University Press, 0021-9525/2000//209 $5.00
The Journal of Cell Biology, Volume 149, Number 1, , 2000 209-222

The Function of Plakophilin 1 in Desmosome Assembly and Actin Filament Organization

^a Molecular Biology Group of the Medical Faculty, University of Halle, 06097 Halle/Saale, Germany
Molecular Biology Group of the Medical Faculty, University of Halle, Magdeburger Strasse 18, 06097 Halle/Saale, Germany.49-345-557-442149-345-557-4422

mechthild.hatzfeld{at}medizin.uni-halle.de

Plakophilin 1, a member of the armadillo multigene family, is a protein with dual localization in the nucleus and in desmosomes. To elucidate its role in desmosome assembly and regulation, we have analyzed its localization and binding partners in vivo. When overexpressed in HaCaT keratinocytes, plakophilin 1 localized to the nucleus and to desmosomes, and dramatically enhanced the recruitment of desmosomal proteins to the plasma membrane. This effect was mediated by plakophilin 1's head domain, which interacted with desmoglein 1, desmoplakin, and keratins in the yeast two-hybrid system. Overexpression of the armadillo repeat domain induced a striking dominant negative phenotype with the formation of filopodia and long cellular protrusions, where plakophilin 1 colocalized with actin filaments. This phenotype was strictly dependent on a conserved motif in the center of the armadillo repeat domain. Our results demonstrate that plakophilin 1 contains two functionally distinct domains: the head domain, which could play a role in organizing the desmosomal plaque in suprabasal cells, and the armadillo repeat domain, which might be involved in regulating the dynamics of the actin cytoskeleton.

Key Words: keratinocytes • desmoglein • armadillo • cell adhesion • cell motility

© 2000 The Rockefeller University Press

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