Huynh-Do, Uyen; Vindis, Cécile; Liu, Hua; Cerretti, Douglas Pat; McGrew, Jeffrey T; Enriquez, Miriam; Chen, Jin; Daniel, Thomas O (2002). Ephrin-B1 transduces signals to activate integrin-mediated migration, attachment and angiogenesis. Journal of cell science, 115(Pt 15), pp. 3073-3081. Company of Biologists Limited
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Ephrin-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.
Item Type: |
Journal Article (Original Article) |
|---|---|
Division/Institute: |
04 Faculty of Medicine > Department of Dermatology, Urology, Rheumatology, Nephrology, Osteoporosis (DURN) > Clinic of Nephrology and Hypertension |
UniBE Contributor: |
Huynh-Do, Uyen |
Subjects: |
600 Technology > 610 Medicine & health |
ISSN: |
0021-9533 |
Publisher: |
Company of Biologists Limited |
Language: |
English |
Submitter: |
Uyen Huynh-Do |
Date Deposited: |
17 Jun 2015 08:40 |
Last Modified: |
05 Dec 2022 14:47 |
PubMed ID: |
12118063 |
BORIS DOI: |
10.7892/boris.69623 |
URI: |
https://boris.unibe.ch/id/eprint/69623 |
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