| First Author | Yang XH | Year | 1997 |
| Journal | Biochem Biophys Res Commun | Volume | 232 |
| Issue | 2 | Pages | 336-9 |
| PubMed ID | 9125176 | Mgi Jnum | J:38958 |
| Mgi Id | MGI:86344 | Doi | 10.1006/bbrc.1997.6284 |
| Citation | Yang XH, et al. (1997) Novel phosphorylated forms of E2F-1 transcription factor bind to the retinoblastoma protein in cells overexpressing an E2F-1 cDNA. Biochem Biophys Res Commun 232(2):336-9 |
| abstractText | In cells overexpressing an exogenous cDNA encoding the E2F-1 transcription factor, as many as eight closely-migrating protein bands were detected after denaturing protein gel electrophoresis and immunoblotting with an E2F-1-specific antibody. Control cells, not overexpressing an E2F-1 cDNA, contained only four E2F-1 specific bands. Pretreatment of protein extracts, from both control and E2F-1 overexpressing cells, with lambda-phosphatase eliminated all E2F-1-specific bands except the single band migrating most rapidly on the gels. These data demonstrated that the multiple protein bands were differentially-phosphorylated forms of E2F-1 protein and showed that novel, more highly phosphorylated E2F-1 forms were present in cells overexpressing the E2F-1 protein. In addition, immunoprecipitation of the retinoblastoma (pRb) protein from cells overexpressing the E2F-1 cDNA showed that the novel, highly phosphorylated E2F-1 forms were preferentially coimmunoprecipitated, indicating that pRb bound preferentially to these E2F-1 forms. |
