Linked Life Data

12118063

Source:http://linkedlifedata.com/resource/pubmed/id/12118063

Statements in which the resource exists.
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pubmed-article:12118063pubmed:abstractTextEphrin-B/EphB family proteins are implicated in bidirectional signaling and were initially defined through the function of their ectodomain sequences in activating EphB receptor tyrosine kinases. Ephrin-B1-3 are transmembrane proteins sharing highly conserved C-terminal cytoplasmic sequences. Here we use a soluble EphB1 ectodomain fusion protein (EphB1/Fc) to demonstrate that ephrin-B1 transduces signals that regulate cell attachment and migration. EphB1/Fc induced endothelial ephrin-B1 tyrosine phosphorylation, migration and integrin-mediated (alpha(v)beta(3) and alpha(5)beta(1)) attachment and promoted neovascularization, in vivo, in a mouse corneal micropocket assay. Activation of ephrin-B1 by EphB1/Fc induced phosphorylation of p46 JNK but not ERK-1/2 or p38 MAPkinases. By contrast, mutant ephrin-B1s bearing either a cytoplasmic deletion (ephrin-B1DeltaCy) or a deletion of four C-terminal amino acids (ephrin-B1DeltaPDZbd) fail to activate p46 JNK. Transient expression of intact ephin-B1 conferred EphB1/Fc migration responses on CHO cells, whereas the ephrin-B1DeltaCy and ephrin-B1DeltaPDZbd mutants were inactive. Thus ephrin-B1 transduces 'outside-in' signals through C-terminal protein interactions that affect integrin-mediated attachment and migration.lld:pubmed
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pubmed-article:12118063pubmed:dateRevised2009-11-19lld:pubmed
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pubmed-article:12118063pubmed:articleTitleEphrin-B1 transduces signals to activate integrin-mediated migration, attachment and angiogenesis.lld:pubmed
pubmed-article:12118063pubmed:affiliationVanderbilt-Ingram Cancer Center, Departments of Medicine, Vanderbilt University Medical Center, Nashville, TN 37232, USA.lld:pubmed
pubmed-article:12118063pubmed:publicationTypeJournal Articlelld:pubmed
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