| First Author | Schreiber-Agus N | Year | 1995 |
| Journal | Cell | Volume | 80 |
| Issue | 5 | Pages | 777-86 |
| PubMed ID | 7889571 | Mgi Jnum | J:31509 |
| Mgi Id | MGI:79018 | Doi | 10.1016/0092-8674(95)90356-9 |
| Citation | Schreiber-Agus N, et al. (1995) An amino-terminal domain of Mxi1 mediates anti-Myc oncogenic activity and interacts with a homolog of the yeast transcriptional repressor SIN3. Cell 80(5):777-86 |
| abstractText | Documented interactions among members of the Myc superfamily support a yin-yang model for the regulation of Myc-responsive genes in which transactivation-competent Myc-Max heterodimers are opposed by repressive Mxi1-Max or Mad-Max complexes. Analysis of mouse mxi1 has led to the identification of two mxi1 transcript forms possessing open reading frames that differ in their capacity to encode a short amino-terminal alpha-helical domain. The presence of this segment dramatically augments the suppressive potential of Mxi1 and allows for association with a mammalian protein that is structurally homologous to the yeast transcriptional repressor SIN3. These findings provide a mechanistic basis for the antagonistic actions of Mxi1 on Myc activity that appears to be mediated in part through the recruitment of a putative transcriptional repressor. |
