Bmx is a downstream Rap1 effector in VEGF-induced endothelial cell activation.
We had previously shown that Rap1 mediates certain of the signaling pathways involved in VEGF-induced endothelial cell migration, although the downstream Rap1 effectors are not known. Towards the goal of identifying those effectors, we utilized a commercially available antibody array filter to identify proteins that either directly interact with Rap1 ... or interact indirectly through a multi-protein complex. The protocol identified 10 possible Rap1-interacting proteins, including the Bmx non-receptor tyrosine kinase. The conclusion that VEGF treatment leads to a Rap1/Bmx complex was confirmed by an experiment in which cell lysates from VEGF and control cells were immunoprecipitated with Bmx antibodies and Western blotting was done using anti-Rap1 antibodies. VEGF treatment led to the recruitment of Bmx to the CAS scaffolding protein, and inhibition of the Bmx kinase blocked VEGF-induced cell migration. Formation of a Rap1/Bmx complex was not observed in cells transfected with an expression vector for a dominant-negative Rap1, indicating that Bmx is a downstream Rap1 effector in VEGF-induced endothelial cell activation.
Mesh Terms:
Cell Movement, Cells, Cultured, Endothelial Cells, Humans, Umbilical Veins, Vascular Endothelial Growth Factor A, rap1 GTP-Binding Proteins
Cell Movement, Cells, Cultured, Endothelial Cells, Humans, Umbilical Veins, Vascular Endothelial Growth Factor A, rap1 GTP-Binding Proteins
Biochem. Biophys. Res. Commun.
Date: Jul. 16, 2004
PubMed ID: 15207703
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