Tyrosine-protein kinase B-Raf (BRAF)

Tyrosine-protein kinase B-Raf (BRAF) is a member of the RAF family of serine/threonine kinases that play a key role in regulating the MAP kinase/ERK signaling pathway, which controls cell division, differentiation, and secretion[1][6][7]. BRAF is composed of three conserved domains (CR1, CR2, CR3), with CR1 and CR2 serving as regulatory regions and CR3 containing the kinase domain[1][2]. When activated by binding of RAS-GTP, BRAF phosphorylates MEK kinases, propagating mitogenic signals from the cell membrane to the nucleus[1][2][7]. Activating mutations in BRAF, notably V600E, drive many cancers by constitutive activation of downstream signaling and uncontrolled proliferation[2][4]. BRAF is the target of several clinically approved kinase inhibitors that selectively inhibit mutant BRAF, providing personalized therapy for patients with BRAF-mutated tumors. BRAF mutations are key diagnostic and predictive biomarkers in cancer, though their targeting is associated with resistance and notable safety considerations.

Other names

B-RafBRAF1proto-oncogene B-RafSerine/threonine-protein kinase B-Raf

Inhibition of mutant BRAF kinase activity (esp. V600E mutation), inhibition of MAPK/ERK signaling pathway, some act as ATP-competitive inhibitors