Functional interaction between SEL-10, an F-box protein, and the nuclear form of activated Notch1 receptor.
作者： Neetu Gupta-Rossi , Odile Le Bail , Hedva Gonen , Christel Brou , Frédérique Logeat
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摘要: The Notch signaling pathway is essential in many cell fate decisions invertebrates as well vertebrates. After ligand binding, a two-step proteolytic cleavage releases the intracellular part of receptor which translocates to nucleus and acts transcriptional activator. Although Notch-induced transcription genes has been reported extensively, its endogenous nuclear form seldom visualized. We report that domain Notch1 stabilized by proteasome inhibitors substrate for polyubiquitination vitro. SEL-10, an F-box protein Cdc4 family, was isolated genetic screen Lin12/Notch-negative regulators Caenorhabditis elegans. human murine counterparts SEL-10 investigated role dominant-negative this protein, deleted F-box, on stability activity. This molecule could stabilize enhance activity but had no effect inactive membrane-anchored forms receptor. then demonstrated specifically interacts with interaction requires phosphorylation event. Taken together, these data suggest involved shutting off ubiquitin-proteasome-mediated degradation active factor after
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