Document Detail

Targeting of p0071 to desmosomes and adherens junctions is mediated by different protein domains.
MedLine Citation:
PMID:  12615965     Owner:  NLM     Status:  MEDLINE    
p0071, a member of the armadillo protein family, is most closely related to p120(ctn) and the plakophilins 1-3. Whereas plakophilins are desmosomal plaque proteins, p120(ctn) localizes to adherens junctions and interacts with classical cadherins. In contrast, p0071 has been described as a protein with dual localization in adherens junctions and desmosomes depending on the cell type examined. Here we have analyzed the localization of p0071 and its domains in detail. Although by sequence analysis, p0071 is more closely related to the adherens junction proteins p120(ctn), ARVCF and delta-catenin, endogenous p0071 associated preferentially with desmosomes in MCF-7 epithelial cells. Overexpressed p0071 localized along cell borders and overlapped only partially with desmosomal markers but colocalized with non-desmosomal cadherins and recruited cadherins to the membrane. The head domain of p0071 was sufficient for desmosomal targeting, whereas the arm repeat domain associated with adherens junctions and enhanced membrane association of classical cadherins. The tail domain localized preferentially to the nucleus and associated with desmosomes. To examine the mechanism underlying this dual localization more closely we determined binding partners of p0071 by using yeast-two-hybrid and mom-targeting assays. These approaches show that the head domain interacted with desmosomal proteins desmocollin 3a and desmoplakin, whereas the armadillo repeat domain binds to non-desmosomal cadherins. Head and armadillo repeat domains both interacted with plakoglobin by binding to different sites. Our data suggest that, in addition to plakoglobin, p0071 is the second armadillo protein present in both types of adhesive junctions and may play a role in regulating crosstalk between adherens junctions and desmosomes.
Mechthild Hatzfeld; Kathleen J Green; Helmut Sauter
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of cell science     Volume:  116     ISSN:  0021-9533     ISO Abbreviation:  J. Cell. Sci.     Publication Date:  2003 Apr 
Date Detail:
Created Date:  2003-03-04     Completed Date:  2003-12-05     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0052457     Medline TA:  J Cell Sci     Country:  England    
Other Details:
Languages:  eng     Pagination:  1219-33     Citation Subset:  IM    
Institute of Physiological Chemistry, Medical Faculty of the University of Halle, 06097 Halle/Saale, Germany.
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MeSH Terms
Adherens Junctions / metabolism*,  ultrastructure
Binding Sites / physiology
Cadherins / metabolism
Cell Adhesion / physiology
Cell Communication / physiology
Cell Membrane / metabolism*,  ultrastructure
Cytoskeletal Proteins / metabolism*
Desmosomes / metabolism*,  ultrastructure
Epithelial Cells / metabolism*,  ultrastructure
Membrane Glycoproteins / metabolism
Protein Binding / physiology
Protein Structure, Tertiary / physiology
Tumor Cells, Cultured
gamma Catenin
Grant Support
Reg. No./Substance:
0/Cadherins; 0/Cytoskeletal Proteins; 0/DSC3 protein, human; 0/DSP protein, human; 0/Desmocollins; 0/Desmoplakins; 0/Membrane Glycoproteins; 0/PKP4 protein, human; 0/Plakophilins; 0/gamma Catenin

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