| First Author | Helin K | Year | 1993 |
| Journal | Genes Dev | Volume | 7 |
| Issue | 10 | Pages | 1850-61 |
| PubMed ID | 8405995 | Mgi Jnum | J:34027 |
| Mgi Id | MGI:81505 | Doi | 10.1101/gad.7.10.1850 |
| Citation | Helin K, et al. (1993) Heterodimerization of the transcription factors E2F-1 and DP-1 leads to cooperative trans-activation. Genes Dev 7(10):1850-61 |
| abstractText | The E2F transcription factor has been implicated in the regulation of genes whose products are involved in cell proliferation. Two proteins have recently been identified with E2F-like properties. One of these proteins, E2F-1, has been shown to mediate E2F-dependent trans-activation and to bind the hypophosphorylated form of the retinoblastoma protein (pRB). The other protein, murine DP-1, was purified from an E2F DNA-affinity column, and it was subsequently shown to bind the consensus E2F DNA-binding site. To study a possible interaction between E2F-1 and DP-1, we have now isolated a cDNA for the human homolog of DP-1. Human DP-1 and E2F-1 associate both in vivo and in vitro, and this interaction leads to enhanced binding to E2F DNA-binding sites. The association of E2F-1 and DP-1 leads to cooperative activation of an E2F-responsive promoter. Finally, we demonstrate that E2F-1 and DP-1 association is required for stable interaction with pRB in vivo and that trans-activation by E2F-1/DP-1 heterodimers is inhibited by pRB. We suggest that E2F is the activity that is formed when an E2F-1-related protein and a DP-1-related protein dimerize. |
