Regulation of cell fate determination by Skp1-Cullin1-F-box (SCF) E3 ubiquitin ligases.

The developing embryo is patterned by a complex set of signals and interactions resulting in changes in cell division, cell fate determination and differentiation. An increasing body of evidence points to the role of the ubiquitin proteasome system (UPS) and ubiquitin-mediated protein degradation as a major mechanism of protein regulation, crucial for control of developmental processes. The specific and irreversible signal generated by protein degradation can function as an integrator of cell signaling events, coupled with other post-translational protein modifications, but also as a master switch for differentiation in its own right. The UPS also displays more subtle mechanisms of regulating signaling than decreasing protein levels, such as proteolytic processing and altering subcellular localization. In particular, the SCF E3 ligase family plays pivotal roles in regulating diverse developmental events in varied species. This review will focus on the role played by SCF E3 ligases in cell fate determination and differentiation.