BRAF is a serine/threonine protein kinase that functions as a key signal transducer in the MAPK cascade. It phosphorylates MAP2K1 to activate the MAP kinase signal transduction pathway 12 and also phosphorylates PFKFB2 3, playing critical roles in mitogenic signaling from the cell membrane to the nucleus. The protein exhibits calcium ion binding and may contribute to hippocampal neuron postsynaptic responses 4. Oncogenic BRAF mutations, particularly the V600E variant occurring through UV-induced DNA damage 5, constitute a major cancer driver across multiple tumor types 6. BRAFV600E induces constitutive kinase activation and is frequently expressed in melanoma, thyroid cancer, and other malignancies 78. In primary cells, BRAFV600E triggers transient proliferation followed by senescence-like cell cycle arrest 7, but in the context of additional genetic lesions, it promotes full malignant transformation. TERT coexpression with BRAFV600E accelerates thyroid cancer dedifferentiation through enhanced ribosomal biogenesis 9. Clinically, BRAFV600E mutations across solid tumors are now targeted with the FDA-approved combination of dabrafenib and trametinib 10, though resistance mechanisms frequently develop. Notably, approximately 35% of BRAF mutations in cancer are non-V600 class mutations, supporting development of broader therapeutic approaches 6. Multiple BRAF protein isoforms with differential expression across cancer types regulate functional outcomes and treatment resistance 11.