FBXW7 is a substrate recognition component of SCF E3 ubiquitin-ligase complexes that mediates ubiquitination and proteasomal degradation of phosphorylated target proteins 123. Key substrates include oncoproteins (MYC, CCNE1/2, NOTCH1/2, JUN) and metabolic regulators (NR1D1, FASN, EZH2), positioning FBXW7 as a critical tumor suppressor 456. In T-ALL, Aurora B kinase phosphorylation of MYC at serine 67 prevents FBXW7-mediated degradation, promoting leukemogenesis; AURKB inhibition restores MYC degradation 7. FBXW7 loss in colorectal cancer promotes FASN-mediated lipogenesis and tumor growth, particularly when stabilized by CSN6 5. In the tumor microenvironment, FBXW7 depletion in cancer-associated fibroblasts activates KMT2 methyltransferase activity and IL-17 signaling, creating paracrine effects that enhance tumor growth 8. Mechanically overloaded chondrocytes downregulate FBXW7, leading to MKK7 stabilization, JNK activation, and accelerated senescence in osteoarthritis 9. In IBD, elevated FBXW7 in intestinal macrophages promotes CCL2/7 expression via EZH2 degradation, increasing inflammatory cell recruitment 6. FBXW7 mutations appear under positive selection in IBD-affected colon 10, while miR-92a-3p suppresses FBXW7 to promote CRC metastasis and chemotherapy resistance 11. The Trim21-FBXW7 axis regulates intestinal Th17 differentiation through JunB and Rorc modulation 12.