| First Author | Prendergast GC | Year | 1991 |
| Journal | Cell | Volume | 65 |
| Issue | 3 | Pages | 395-407 |
| PubMed ID | 1840505 | Mgi Jnum | J:19400 |
| Mgi Id | MGI:67565 | Doi | 10.1016/0092-8674(91)90457-a |
| Citation | Prendergast GC, et al. (1991) Association of Myn, the murine homolog of max, with c-Myc stimulates methylation-sensitive DNA binding and ras cotransformation. Cell 65(3):395-407 |
| abstractText | Myn, a novel murine approximately 18 kd basic/helix-loop-helix/leucine zipper (B/HLH/LZ) protein, forms a specific DNA-binding complex with the c-Myc oncoprotein through the HLH/LZ motif in both proteins. c-Myc/Myn recognizes a c-Myc-binding site (GACCACGTGGTC) with higher affinity than either protein by itself. CpG methylation of the recognition site greatly inhibits DNA binding, suggesting that DNA methylation may regulate the c-Myc/Myn complex in vivo. In 3T3 fibroblasts, Myn mRNA levels are induced several-fold by serum with delayed early kinetics, suggesting regulation by immediate-early gene products. Coexpression of Myn in a myc/ras rat embryo fibroblast focus formation assay specifically augmented c-myc transforming activity. We suggest that interaction of Myn with c-Myc stabilizes sequence-specific DNA binding in vivo. |
