F-box and leucine-rich repeat protein 7 (FBXL7)

F-box and leucine-rich repeat protein 7 (FBXL7) is a highly conserved member of the F-box protein family characterized by an F-box domain and multiple leucine-rich repeats. FBXL7 functions as a substrate-recognition subunit of the SCF E3 ubiquitin ligase complex, mediating the polyubiquitylation and proteasomal degradation of diverse protein substrates, notably including the mitotic kinase Aurora A, c-Src, Survivin, and Snail1. This activity allows FBXL7 to regulate essential cellular processes such as cell cycle progression, apoptosis, cell migration, invasion, DNA damage response, and glucose metabolism. Dysregulated FBXL7 expression or function is linked to various pathologies, including tumorigenesis, metastasis, drug resistance in cancer, and Hennekam syndrome. FBXL7’s expression and mutational status are explored as biomarkers for cancer prognosis. Its dual role—acting as either a tumor suppressor or, contextually, as an oncoprotein—calls for careful therapeutic consideration.

Other names

F-box/LRR-repeat protein 7FBXL7FBL6FBL7KIAA0840F-box protein FBL6/FBL7F-box protein Fbl7

Drugs (potential/experimental) would modulate proteasomal degradation of targets through inhibition/stabilization of FBXL7’s E3 ligase function. Affecting substrate ubiquitylation impacting cell cycle, apoptosis, and metastasis.