Defining desmosomal plakophilin-3 interactions

Stefan Bonné, Barbara Gilbert, Mechthild Hatzfeld, Xinyu Chen, Kathleen J. Green, Frans Van Roy*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

103 Scopus citations

Abstract

Plakophilin 3 (PKP3) is a recently described armadillo protein of the desmosomal plaque, which is synthesized in simple and stratified epithelia. We investigated the localization pattern of endogenous and exogenous PKP3 and fragments thereof. The desmosomal binding properties of PKP3 were determined using yeast two-hybrid, coimmuno-precipitation and colocalization experiments. To this end, novel mouse anti-PKP3 mAbs were generated. We found that PKP3 binds all three desmogleins, desmocollin (Dsc) 3a and -3b, and possibly also Dsc1a and -2a. As such, this is the first protein interaction ever observed with a Dsc-b isoform. Moreover, we determined that PKP3 interacts with plakoglobin, desmoplakin (DP) and the epithelial keratin 18. Evidence was found for the presence of at least two DP-PKP3 interaction sites. This finding might explain how lateral DP-PKP interactions are established in the upper layers of stratified epithelia, increasing the size of the desmosome and the number of anchoring points available for keratins. Together, these results show that PKP3, whose epithelial and epidermal desmosomal expression pattern and protein interaction repertoire are broader than those of PKP1 and -2, is a unique multiprotein binding element in the basic architecture of a vast majority of epithelial desmosomes.

Original languageEnglish (US)
Pages (from-to)403-416
Number of pages14
JournalJournal of Cell Biology
Volume161
Issue number2
DOIs
StatePublished - Apr 28 2003

Keywords

  • Armadillo
  • Cell adhesion
  • Desmosomes
  • Protein interaction
  • Tw-hybrid system

ASJC Scopus subject areas

  • Cell Biology

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