About EPH Receptor:
Erythropoietin-producing hepatocellular carcinoma receptors, also known as Eph receptors, make up the largest subfamily of receptor tyrosine kinases. By 1987, research had shown that this group of receptors is linked with proliferative diseases such as cancer. Over the years, scientists have been seeking to gain more information on these relatively complex receptors.
Eph Receptor Structure
The Eph receptors are the largest receptor tyrosine kinases (RTKs) subfamily because they consist of fourteen members classified under EphA and EphB subgroups. The various members are categorized based on their extracellular surface sequence homology and their preference to react to either the EphA or EphB ligands. However, it has been seen that promiscuous binding may occur; that is, EphA receptors can bind with EphB ligands, and EphB receptors can bind with EphA ligands. Through research such as the chimera experiment, scientists have discovered that promiscuous binding may create broader signaling functions for the Eph receptor.
Eph Receptor Functions
Since the Eph ligands are of a membrane-tethered nature, they are responsible for their Eph receptor’s ability to initiate intercellular signaling events upon cell-cell contact. These signaling events include but are not limited to axonal guidance, neural plasticity, angiogenesis, tissue patterning, and cell migration. Although it was initially believed that Eph receptors drive signaling using catalytic activities, research has shown that some receptors in the family have non-catalytic functions in the signaling process. For example, EphA10 and EphB4 have been found to have an absence in the amino acids needed to carry out a catalyze reaction. Such receptors are known as pseudokinases.