Source:http://linkedlifedata.com/resource/pubmed/id/10373410
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
26
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pubmed:dateCreated |
1999-7-15
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pubmed:abstractText |
The contribution of desmosomes to epidermal integrity is evident in the inherited blistering disorder associated with the absence of a functional gene for plakophilin-1. To define the function of plakophilin-1 in desmosome assembly, interactions among the desmosomal cadherins, desmoplakin, and the armadillo family members plakoglobin and plakophilin-1 were examined. In transient expression assays, plakophilin-1 formed complexes with a desmoplakin amino-terminal domain and enhanced its recruitment to cell-cell borders; this recruitment was not dependent on the equimolar expression of desmosomal cadherins. In contrast to desmoplakin-plakoglobin interactions, the interaction between desmoplakin and plakophilin-1 was not mediated by the armadillo repeat domain of plakophilin-1 but by the non-armadillo head domain, as assessed by yeast two-hybrid and recruitment assays. We propose a model whereby plakoglobin serves as a linker between the cadherins and desmoplakin, whereas plakophilin-1 enhances lateral interactions between desmoplakin molecules. This model suggests that epidermal lesions in patients lacking plakophilin-1 are a consequence of the loss of integrity resulting from a decrease in binding sites for desmoplakin and intermediate filaments at desmosomes.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Desmoplakins,
http://linkedlifedata.com/resource/pubmed/chemical/Plakophilins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/gamma Catenin
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
274
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
18145-8
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:10373410-Animals,
pubmed-meshheading:10373410-COS Cells,
pubmed-meshheading:10373410-Cell Adhesion Molecules,
pubmed-meshheading:10373410-Cytoskeletal Proteins,
pubmed-meshheading:10373410-Desmoplakins,
pubmed-meshheading:10373410-Desmosomes,
pubmed-meshheading:10373410-Plakophilins,
pubmed-meshheading:10373410-Protein Binding,
pubmed-meshheading:10373410-Protein Conformation,
pubmed-meshheading:10373410-Proteins,
pubmed-meshheading:10373410-Rabbits,
pubmed-meshheading:10373410-Skin Diseases,
pubmed-meshheading:10373410-gamma Catenin
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pubmed:year |
1999
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pubmed:articleTitle |
The head domain of plakophilin-1 binds to desmoplakin and enhances its recruitment to desmosomes. Implications for cutaneous disease.
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pubmed:affiliation |
Department of Dermatology and the Robert H. Lurie Cancer Center, Northwestern University Medical School, Chicago, Illinois 60611, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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