Tyrosine kinase with immunoglobulin and EGF homology domains 2 (Tie-2 (also known as TEK))

Tyrosine kinase with immunoglobulin and EGF homology domains 2—commonly referred to as Tie‑2 or TEK—is a receptor tyrosine kinase primarily expressed on endothelial cells. It features an extracellular region containing two immunoglobulin-like domains flanking three epidermal growth factor (EGF)-like domains followed by three fibronectin type III repeats; intracellularly it has a split tyrosine kinase domain. The main ligands are angiopoietins (ANGPT1/ANGPT2/ANGPT4), which regulate critical processes such as embryonic vasculature formation, postnatal blood vessel maintenance/stability (“vascular quiescence”), endothelial survival/proliferation/migration/adhesion/spreading, actin cytoskeleton reorganization, anti-inflammatory responses via barrier integrity preservation—and overall control of physiological/pathological angiogenesis. Mutations can cause inherited venous malformations. Dysregulation is implicated in cancer progression through abnormal neovascularization.

Other names

Tie-2TEKTunica interna endothelial cell kinaseTyrosine-protein kinase receptor TIE-2CD202b

Drugs targeting this molecule typically act by inhibiting its tyrosine kinase activity or blocking ligand binding to disrupt downstream signaling involved in angiogenesis and vascular maintenance. Some agents may function as antagonists to its ligands such as Angiopoietin‑1/Angiopoietin‑2.