| Targeting of p0071 to desmosomes and adherens junctions is mediated by different protein domains. | |
MedLine Citation:
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PMID: 12615965 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
Authors:
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Mechthild Hatzfeld; Kathleen J Green; Helmut Sauter |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Journal of cell science Volume: 116 ISSN: 0021-9533 ISO Abbreviation: J. Cell. Sci. Publication Date: 2003 Apr |
Date Detail:
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Created Date: 2003-03-04 Completed Date: 2003-12-05 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 0052457 Medline TA: J Cell Sci Country: England |
Other Details:
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Languages: eng Pagination: 1219-33 Citation Subset: IM |
Affiliation:
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Institute of Physiological Chemistry, Medical Faculty of the University of Halle, 06097 Halle/Saale, Germany. mechthild.hatzfeld@medizin.uni-halle.de |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Adherens Junctions
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metabolism*,
ultrastructure Animals Binding Sites / physiology Cadherins / metabolism Cell Adhesion / physiology Cell Communication / physiology Cell Membrane / metabolism*, ultrastructure Cytoskeletal Proteins / metabolism* Desmocollins Desmoplakins Desmosomes / metabolism*, ultrastructure Epithelial Cells / metabolism*, ultrastructure Humans Membrane Glycoproteins / metabolism Plakophilins Protein Binding / physiology Protein Structure, Tertiary / physiology Tumor Cells, Cultured gamma Catenin |
| Grant Support | |
ID/Acronym/Agency:
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AR43380/AR/NIAMS NIH HHS; P01 DE12328/DE/NIDCR NIH HHS |
| Chemical | |
Reg. No./Substance:
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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 |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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