title: Ubiquitination of Myc: flipping the switch.
abstract: Ubiquitination plays a key role in regulating multiple oncoproteins, including those of the Myc-family. A recent Cell paper by Adhikary et al reports that a novel E3 ligase, HectH9, mediates site-specific ubiquitination of Myc and thereby fosters a switch from repression to transcriptional activation. This insight elucidates Myc's diverse properties and provides new targets for the development of anti-cancer therapy.
authors.affiliation: University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104, USA.
authors.forename: Amelie
authors.initials: A
authors.lastname: Boquoi
authors.forename: Gregory
authors.initials: G
authors.lastname: Enders
mesh_terms: D000818:Animals; D015972:Gene Expression Regulation, Neoplastic; D006801:Humans; D011499:Protein Processing, Post-Translational; D016271:Proto-Oncogene Proteins c-myc / Q000378:metabolism*; D014158:Transcription, Genetic; D015533:Transcriptional Activation; D025801:Ubiquitin / Q000378:metabolism*; D044767:Ubiquitin-Protein Ligases / Q000502:physiology
chemical_list: D016271:Proto-Oncogene Proteins c-myc; D025801:Ubiquitin; D044767:Ubiquitin-Protein Ligases