PDGFRA is a tyrosine-protein kinase receptor that serves as a cell-surface receptor for PDGFA, PDGFB, and PDGFC ligands, playing essential roles in embryonic development, cell proliferation, survival, and chemotaxis 1. Upon ligand binding, PDGFRA activates multiple downstream signaling cascades including PI3K/AKT, MAPK/ERK, and STAT pathways through phosphorylation of PIK3R1, PLCG1, and PTPN11 [UniProt]. The receptor regulates diverse physiological processes including mesenchymal stem cell differentiation, skeleton development, gastrointestinal mucosal development, wound healing, and platelet aggregation [UniProt]. Clinically, PDGFRA is highly relevant to cancer pathogenesis. Amplification of the PDGFRA locus on chromosome 4 is frequently observed in glioblastomas (GBM), with PDGFRA amplification correlating with poor prognosis when co-amplified with KIT and KDR 2. In GBM, PDGFRA functions cooperatively with EPHA2 to promote cell proliferation, and dual PDGFRA/EPHA2 inhibition shows superior therapeutic efficacy compared to PDGFRA inhibition alone 3. Additionally, germline PDGFRA mutations cause PDGFRA-mutant syndrome, characterized by multiple gastrointestinal mesenchymal tumors including inflammatory fibroid polyps and gastric GISTs 4. PDGFRA mutations are also identified in eosinophilic myeloid disorders 5, establishing this receptor as a critical therapeutic target across multiple malignancies.