KIT proto-oncogene tyrosine-protein kinase receptor (KIT (also commonly referred to as c-KIT))

KIT proto-oncogene tyrosine-protein kinase receptor (KIT or c-KIT) is a cell surface receptor tyrosine kinase (type III family) encoded by the KIT gene. It binds the stem cell factor (SCF) ligand, inducing dimerization and activation of intrinsic kinase activity, leading to autophosphorylation and triggering multiple downstream signaling cascades (e.g., PI3K/AKT, Ras/MAPK, Src family kinases). KIT plays crucial roles in normal hematopoiesis, gametogenesis, pigmentation, and mast cell biology. Oncogenic mutations and overexpression of KIT drive important roles in various tumors—notably gastrointestinal stromal tumors (GIST), some leukemias, melanomas, and others. KIT is a validated drug target, with several tyrosine kinase inhibitors (e.g., imatinib, sunitinib) approved for treatment of KIT-driven cancers. Detection of KIT protein (CD117) and genotyping of KIT mutations function as both diagnostic and predictive biomarkers. Therapeutic challenges include primary and acquired resistance to kinase inhibitors and management of side effects due to inhibition of KIT in normal tissues[1][3][4][6][7][9].

Other names

c-KITCD117Mast/stem cell growth factor receptor (SCFR)Stem cell factor receptorProto-oncogene c-KIT

Tyrosine kinase inhibition: Drugs bind to the ATP-binding site of the kinase domain, blocking kinase activity and downstream signaling[4][6].