ANKS1A, also known as Odin, functions as an effector of epidermal derived growth factor receptor (EGFR) recycling [], interacts with 14-3-3 proteins []and restricts platelet-derived growth factor (PDGF)-mediated cell proliferation [].Structurally, it consist of N-terminal ankyrin motifs followed by tandem sterile alpha motif (SAM) domains and a carboxyl phosphotyrosine binding (PTB) domain []. The PTB domain has been shown to be crucial for association with the juxtamembrane domain of ephrin receptor EphA8 [], and the SAM domain is involved in modulating its degradation [], thereby regulating EphA signalling.
This entry represents the ligand-binding domain found in ephrin type-A receptor 8 (EphA8), also known as EEK. EphA8 has been suggested to play a role in axonal pathfinding during nervous system development in mammals [], as well as being implicated in cancer [].Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands [, ]. Ephrin receptors (EphRs) comprise the largest subfamily of receptor tyrosine kinases (RTKs). EphRs contain a ligand binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyrosine kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling) [].
