Defining desmosomal plakophilin-3 interactions

被引:128
作者
Bonné, S
Gilbert, B
Hatzfeld, M
Chen, X
Green, KJ
van Roy, F
机构
[1] Univ Ghent, Dept Mol Biomed Res,Mol Cell Biol Unit, B-9000 Ghent, Belgium
[2] Univ Halle Wittenberg, Inst Physiol Chem, Fac Med, Mol Biol Grp, D-06097 Halle An Der Saale, Germany
[3] Northwestern Univ, Feinberg Sch Med, Dept Pathol, Chicago, IL 60611 USA
[4] Northwestern Univ, Feinberg Sch Med, Dept Dermatol, Chicago, IL 60611 USA
[5] Northwestern Univ, Feinberg Sch Med, Robert H Lurie Comprehens Canc Ctr, Chicago, IL 60611 USA
关键词
armadillo; cell adhesion; desmosomes; protein interaction; two-hybrid system;
D O I
10.1083/jcb.200303036
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
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, coimmunoprecipitation 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.
引用
收藏
页码:403 / 416
页数:14
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