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Papers In Press, published online ahead of print November 16, 2001
Department of Immunology and Allergy, The Hospital for Sick Children, Toronto, Ontario M5G 1X8
Corresponding Author: chaim.roifman{at}sickkids.ca
Uniquely for the Eph family of receptor tyrosine kinases, the EphB6 receptor is catalytically inactive due to the alteration of several critical residues in its kinase domain. This has cast doubt upon its ability to participate in cytoplasmic signaling events. We show here that despite its lack of kinase activity EphB6 undergoes inducible tyrosine phosphorylation upon stimulation with the Eph-B receptor subfamily ligand ephrin-B1. We also demonstrate, for the first time, evidence of cross-talk between Eph receptors. Overexpression of a catalytically active member of the Eph-B subfamily, EphB1, resulted in increased EphB6 phosphorylation. EphB1 induced EphB6 phosphorylation was ligand dependent and required the functional catalytic activity of EphB1. EphB1 not only transphosphorylated EphB6, but together they also formed a stable hetero-complex. In addition, we identify the proto-oncogene c-Cbl as an EphB6 binding protein. Although EphB6-Cbl association appeared to be constitutive, Cbl required a functional phosphotyrosine binding (PTB) domain in order to bind the receptor, while its RING finger motif ubiquitin-transfer domain was not necessary. Our findings demonstrate that EphB6 is an actively signaling receptor that undergoes trans-phosphorylation upon ligand binding, and can initiate specific cytoplasmic signaling events.
J. Biol. Chem, 10.1074/jbc.M108011200
Submitted on August 20, 2001
Revised on November 1, 2001
Accepted on November 15, 2001
The kinase null EphB6 receptor undergoes trans-phosphorylation in a complex with EphB1
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