F-box and leucine-rich repeat protein 17 (FBXL17)

F-box and leucine-rich repeat protein 17 (FBXL17) is a substrate-recognition component of the SCF (SKP1–Cullin–F-box) E3 ubiquitin ligase complex, part of the F-box protein family characterized by the presence of an F-box motif and leucine-rich repeats. FBXL17 mediates the ubiquitination and proteasomal degradation of key regulatory proteins, including suppressor of fused (SUFU) in the Hedgehog signaling pathway, histone methyltransferase PRMT1, and aberrant BTB-domain protein dimers. It controls cell proliferation, is essential for neural cell survival, and acts as a regulator (and sometimes oncogene) in certain cancers such as medulloblastoma and breast cancer. FBXL17 also interacts with UAP1 to modulate O-GlcNAcylation, maintaining cellular protein modification balance. Its structure is defined by a characteristic leucine-rich repeat "horseshoe" domain enabling substrate binding; mutations affecting these domains are linked to altered cancer risk. FBXL17 is a potential therapeutic target for drug development, but clinical agents are not yet identified.

Other names

FBL17FBX13DKFZP434C1715Fbx13Fbl17F-box/LRR-repeat protein 17F-box only protein 13FBXO13

Drugs (experimental or theoretical) would act by inhibiting FBXL17 ubiquitin ligase activity, blocking substrate degradation, or altering associated signaling pathways (e.g., Hedgehog signaling)