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Research Article |
1 Vanderbilt-Ingram Cancer Center, Departments of Medicine, Vanderbilt
University Medical Center, Nashville, TN 37232, USA
2 Division of Nephrology and Hypertension, Department of Medicine and Clinical
Research, University of Bern, CH-3010 Bern, Switzerland
3 Immunex Corporation, Seattle, WA 98101, USA
4 Cancer Biology, Vanderbilt University Medical Center, Nashville, TN 37232
USA
5 Cell Biology, Vanderbilt University Medical Center, Nashville, TN 37232,
USA
* Author for correspondence (e-mail: jin.chen{at}mcmail.vanderbilt.edu )
Accepted 16 May 2002
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 (
vß3 and
5ß1) 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-B1
Cy) or a deletion of four C-terminal amino acids
(ephrin-B1PDZbd) fail to activate p46 JNK. Transient expression of
intact ephin-B1 conferred EphB1/Fc migration responses on CHO cells, whereas
the ephrin-B1Cy and ephrin-B1PDZbd mutants were inactive. Thus
ephrin-B1 transduces `outside-in' signals through C-terminal protein
interactions that affect integrin-mediated attachment and migration.
Key words: Ephrin-B1, EphB1, Endothelial, Angiogenesis, Signal transduction
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