FBXO40 Inhibitors

FBXO40 is a component of the Skp1-Cullin 1-F-box (SCF) E3 ubiquitin ligase complex, a crucial machinery responsible for ubiquitinating specific target proteins and marking them for degradation by the proteasome. In the context of the SCF complex, FBXO40 acts as the F-box protein, which provides substrate specificity by recognizing and binding to specific target proteins. The binding of FBXO40 to its target proteins leads to their ubiquitination, ultimately regulating their stability and cellular levels. Inhibitors of FBXO40 disrupt the interaction between FBXO40 and its specific substrate proteins, thus interfering with the ubiquitination and subsequent degradation of these substrates. The precise mechanisms by which FBXO40 inhibitors achieve this interference are areas of ongoing research. Understanding the functions and regulatory roles of FBXO40 within the SCF E3 ubiquitin ligase complex can provide valuable insights into the intricate machinery governing protein turnover and degradation in cells, shedding light on the broader mechanisms that control cellular processes and homeostasis.