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J. Biol. Chem., Vol. 277, Issue 6, 3823-3828, February 8, 2002
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From the Immunology and Allergy, Department of Paediatrics,
Infection, Immunity, Injury and Repair Program, Research Institute,
The Hospital for Sick Children and the University of Toronto,
Toronto M5G 1X8, Canada
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
domain in order to bind the receptor, whereas its RING finger motif
ubiquitin-transfer domain was not necessary. Our findings demonstrate
that EphB6 is an actively signaling receptor that undergoes
transphosphorylation upon ligand binding and that can initiate specific
cytoplasmic signaling events.
The Kinase-null EphB6 Receptor Undergoes
Transphosphorylation in a Complex with EphB1*
,, and
*
This work was supported by a grant from the National Cancer
Institute of Canada.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
These authors contributed equally to this work.
§
The Donald and Audrey Campbell Chair of Immunology. To whom
correspondence should be addressed: Div. of Immunology and Allergy, Dept. of Paediatrics, Infection, Immunity, Injury and Repair Program, The Research Institute of Hospital for Sick Children, 555 University Ave., Toronto, Ontario M5G 1X8, Canada; Tel.: 1-416-813-8623; Fax:
1-416-813-8624; E-mail: croifman@sickkids.on.ca.
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