Linked Life Data

10564659

Source:http://linkedlifedata.com/resource/pubmed/id/10564659

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2000-2-3
pubmed:abstractText
Lateral clustering of E-cadherin molecules is required for the adhesive properties of this cell-cell adhesion molecule. Both the extracellular domain and the cytoplasmic region of E-cadherin were previously reported to contribute to lateral clustering, but little is known about a role of the transmembrane domain in this respect. Following our previous findings indicating self-assembly of artificial transmembrane segments based on leucine residues, we asked whether the leucine-rich transmembrane segment of E-cadherin participates in lateral clustering. Here, we demonstrate that its transmembrane domain self-assembles as analyzed using the ToxR reporter system. Certain point mutations within the transmembrane domain markedly reduced self-assembly. To study whether the same point mutations also affect E-cadherin-mediated adhesion in vivo, wild-type and mutant E-cadherin cDNAs were transfected into Ltk(-) cells. Indeed, cell aggregation assays revealed significantly reduced adhesiveness when mutations had been introduced which disrupted transmembrane segment interaction. In control experiments, cell-surface expression, interaction with catenins and the cytoskeleton as well as trypsin-resistance of the protein were unaffected. These data suggest that interactions between the transmembrane segments are important for the lateral association of E-cadherin molecules required for cell-cell adhesion.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9533
pubmed:author
pubmed:issnType
Print
pubmed:volume
112 ( Pt 23)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4415-23
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:10564659-Amino Acid Sequence, pubmed-meshheading:10564659-Animals, pubmed-meshheading:10564659-Bacterial Proteins, pubmed-meshheading:10564659-Cadherins, pubmed-meshheading:10564659-Cell Adhesion, pubmed-meshheading:10564659-Cell Aggregation, pubmed-meshheading:10564659-DNA-Binding Proteins, pubmed-meshheading:10564659-Genes, Reporter, pubmed-meshheading:10564659-L Cells (Cell Line), pubmed-meshheading:10564659-Mice, pubmed-meshheading:10564659-Models, Molecular, pubmed-meshheading:10564659-Molecular Sequence Data, pubmed-meshheading:10564659-Mutagenesis, Site-Directed, pubmed-meshheading:10564659-Recombinant Fusion Proteins, pubmed-meshheading:10564659-Transcription Factors, pubmed-meshheading:10564659-Transcriptional Activation, pubmed-meshheading:10564659-Transfection
pubmed:year
1999
pubmed:articleTitle
Mutations affecting transmembrane segment interactions impair adhesiveness of E-cadherin.
pubmed:affiliation
Dept of Clinical Chemistry and Pathobiochemistry, Universitätsklinikum Benjamin Franklin, Hindenburgdamm 30, D-12200 Berlin, Germany. huber@ukbf.fu-berlin.de
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't