Platelet-derived growth factor receptor beta (PDGFRB) (PDGFRB)

Platelet-derived growth factor receptor beta (PDGFR-β) is a transmembrane receptor tyrosine kinase that serves as a critical regulator of mesenchymal cell proliferation, migration, and survival [1, 2, 6]. Upon binding its ligands, primarily PDGF-BB and PDGF-DD, the receptor undergoes dimerization and autophosphorylation, which activates intracellular signaling cascades such as the PI3K/Akt, Ras/MAPK, and PLCγ pathways [1, 5, 8]. These processes are vital for normal physiological functions, including embryonic development, wound healing, and the maintenance of vascular integrity [2, 4, 9]. However, aberrant PDGFR-β signaling—driven by genetic translocations, mutations, or overexpression—is a key driver in several diseases, most notably myeloproliferative neoplasms, gastrointestinal stromal tumors (GIST), and various fibrotic disorders [1, 3, 7, 11]. Because of its central role in disease pathogenesis, PDGFR-β is a primary target for several clinical tyrosine kinase inhibitors, such as imatinib and sunitinib, which competitively inhibit the ATP-binding site of the kinase domain [5, 10, 12]. Therapeutic targeting of this receptor continues to be a focus in oncology and is increasingly being investigated for the treatment of organ fibrosis and pulmonary arterial hypertension [7, 8, 9].

Other names

CD140BPDGFR1JTK12Platelet-derived growth factor receptor 1IBGC4IMF1KOGSPENTTPDGFR-beta

Inhibition of the intracellular tyrosine kinase domain by competing with ATP for the binding site, thereby blocking autophosphorylation and downstream signaling pathways [5, 7, 11].