Linked Life Data

7738346

Source:http://linkedlifedata.com/resource/pubmed/id/7738346

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1995-6-2
pubmed:abstractText
Desmogleins are transmembrane desmosomal cadherins. Two desmogleins, Dsg3 and Dsg1, have been shown to bind plakoglobin, an intracytoplasmic (IC) desmosomal plaque protein. This binding may be critical for desmosome assembly or stability. The IC domain of desmogleins consists of subdomains that are either desmoglein specific or homologous with the IC region of classical cadherins. Here we identify the domains of human Dsg3 that are critical for plakoglobin binding in human keratinocytes. We constructed eukaryotic expression vectors containing chimeric cDNAs that encode the extracellular domain of mouse E-cadherin (Ecad) with the transmembrane and IC domains of Dsg3, with increasing truncations eliminating various IC subdomains from the carboxy-terminus. These constructs were used for transient transfection of HaCaT cells. Extracts were subjected to immunoprecipition with an anti-mouse Ecad antibody (that does not precipitate human Ecad), thus precipitating the chimeric protein and any tightly associated plakoglobin. Co-precipitation of plakoglobin was confirmed by immunoblotting. These data show that the desmoglein-specific IC subdomains are not necessary for plakoglobin binding, but the carboxy-terminal 87 amino acids of the IC-cadherin-like segment subdomain are critical. Finally, we confirmed these results outside cells with in vitro transcription and translation, which also demonstrates that the Dsg3-plakoglobin interaction is direct and does not depend on other cellular factors. These results underscore the importance of a region, highly conserved in all desmogleins, in the carboxy terminus of the IC-cadherin-like subdomain for the localization of plakoglobin to desmosomes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0022-202X
pubmed:author
pubmed:issnType
Print
pubmed:volume
104
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
720-4
pubmed:dateRevised
2005-11-17
pubmed:meshHeading
pubmed-meshheading:7738346-Amino Acid Sequence, pubmed-meshheading:7738346-Autoantigens, pubmed-meshheading:7738346-Cadherins, pubmed-meshheading:7738346-Cell Adhesion Molecules, pubmed-meshheading:7738346-Cell Communication, pubmed-meshheading:7738346-Cell Line, pubmed-meshheading:7738346-Cytoplasm, pubmed-meshheading:7738346-Cytoskeletal Proteins, pubmed-meshheading:7738346-Desmoglein 1, pubmed-meshheading:7738346-Desmoglein 3, pubmed-meshheading:7738346-Desmogleins, pubmed-meshheading:7738346-Desmoplakins, pubmed-meshheading:7738346-Humans, pubmed-meshheading:7738346-Keratinocytes, pubmed-meshheading:7738346-Molecular Sequence Data, pubmed-meshheading:7738346-Pemphigus, pubmed-meshheading:7738346-Protein Binding, pubmed-meshheading:7738346-Subcellular Fractions, pubmed-meshheading:7738346-gamma Catenin
pubmed:year
1995
pubmed:articleTitle
Plakoglobin binding by human Dsg3 (pemphigus vulgaris antigen) in keratinocytes requires the cadherin-like intracytoplasmic segment.
pubmed:affiliation
Dermatology Branch, National Institutes of Health, Bethesda, Maryland, USA.
pubmed:publicationType
Journal Article