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Myc, a transcription factor with oncogenic activity, is upregulated by amplification, translocation and mutation of the cellular pathways that regulate its stability. Inhibition of the Myc oncogene by various modalities has had limited success. One Myc inhibitor, Omomyc, has limited cellular and in vivo activity. Here, we report a mini-protein, referred to as Mad, which is derived from the cellular Myc antagonist Mxd1. Mad localizes to the nucleus in cells and is ten-fold more potent than Omomyc in inhibiting Myc-driven cell proliferation. Similarly to Mxd1, Mad also interacts with Max, the binding partner of Myc, and with the nucleolar upstream binding factor (UBF). Mad binds to E-Box DNA in the promoters of Myc target genes and represses Myc-mediated transcription to a greater extent than Omomyc. Overall, Mad appears to be more potent than Omomyc both in vitro and in cells.
This article was published in the following journal.
Name: FEBS letters
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A tripartite motif protein consisting of an N-terminal RING finger, two B-box type ZINC FINGERS, and C-terminal PHD domain. It functions as a transcriptional repressor by associating with Kruppel-association box domain (KRAB domain) transcription factors and has E3-SUMO-ligase activity towards itself and also sumoylates INTERFERON REGULATORY FACTOR-7 to reduce its activity as a transcriptional activator. It can also function as a ubiquitin protein ligase towards TUMOR SUPPRESSOR PROTEIN P53.
An adaptor protein, consisting of seven WD REPEATS along its length, that functions as a component of the MECHANISTIC TARGET OF RAPAMYCIN COMPLEX 1 and MTORC2 COMPLEX. It interacts directly with MTOR to enhance its kinase activity and stabilizes the MTOR-RPTOR PROTEIN interaction in nutrient-poor conditions, favoring RPTOR inhibition of MTOR activity.
An AT-hook-containing (AT-HOOK MOTIFS) nuclear protein that may be involved in retinoid-dependent transcriptional activity.
A transcription factor that takes part in WNT signaling pathway where it may play a role in the differentiation of KERATINOCYTES. The transcriptional activity of this protein is regulated via its interaction with BETA CATENIN.
A cellular transcriptional coactivator that was originally identified by its requirement for the stable assembly IMMEDIATE-EARLY PROTEINS of the HERPES SIMPLEX VIRUS. It is a nuclear protein that is a transcriptional coactivator for a number of transcription factors including VP16 PROTEIN; GA-BINDING PROTEIN; EARLY GROWTH RESPONSE PROTEIN 2; and E2F4 TRANSCRIPTION FACTOR. It also interacts with and stabilizes HERPES SIMPLEX VIRUS PROTEIN VMW65 and helps regulate GENETIC TRANSCRIPTION of IMMEDIATE-EARLY GENES in HERPES SIMPLEX VIRUS.
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