Not exact matches
Studies by ours and other groups have shown that a number of EphA2 and EphA3 mutations inactivate
Eph receptor canonical signaling by disrupting ephrin binding or
kinase activity, consistent with a role of canonical signaling in tumor suppression.
In addition, at least some
Eph receptors can also signal through non-canonical mechanisms that are independent of ligand binding and
kinase activity, for example through interplay with other receptor tyrosine
kinase families and with serine / threonine
kinases.
These
activities are independent of ephrin binding and / or
kinase activity and their mechanism is not well understood but in some cases depends on
Eph receptor phosphorylation on serine / threonine residues (red circle).
For example, our past work showed that two conserved tyrosine phosphorylation sites in the juxtamembrane segment of the
Eph receptors not only mediate association with binding partners but also regulate receptor
kinase activity.