Abstract
The transcription factor c-Myc is a cellular oncoprotein generally upregulated in most of human cancers. NF-κB essential modulator (NEMO) caused phosphorylation and stabilization of c-Myc protein in the nucleus through direct interaction. The interaction caused reduced ubiquitination of c-Myc by inhibiting ubiquitinating activity of Fbw7 without blocking the interaction between c-Myc and Fbw7. As a consequence, NEMO enhanced the expression of several selected c-Myc targets. Compared to the classical role as an essential subunit for the activity of IKK complex, stabilization of c-Myc by direct interaction is a unique function of NEMO, representing a new mechanism to regulate c-Myc activity. Structured summary MINT- 8045088: c-Myc (uniprotkb: P01106) and NEMO (uniprotkb: Q9Y6K9) colocalize (MI: 0403) by fluorescence microscopy (MI: 0416) MINT- 8045072, MINT- 8045101: c-Myc (uniprotkb: P01106) physically interacts (MI: 0915) with NEMO (uniprotkb: Q9Y6K9) by anti tag coimmunoprecipitation (MI: 0007)
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