This knowledge is useful for the development of disease treatments based on modulating Eph receptor /
ephrin activities.
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.
Binding to
ephrin ligands on the surface of neighboring cells induces canonical signaling involving receptor clustering, autophosphorylation on tyrosine residues, and kinase
activity - dependent downstream signaling.
We found that canonical signaling by the EphB4 receptor is low in breast cancer cells and that
ephrin - induced stimulation of EphB4 kinase
activity inhibits breast cancer cell malignancy in culture and tumor growth in vivo (Figure 1A) through inhibition of the CRK proto - oncogene.
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).