| First Author | Bi B | Year | 2001 |
| Journal | Immunology | Volume | 104 |
| Issue | 1 | Pages | 37-42 |
| PubMed ID | 11576218 | Mgi Jnum | J:71601 |
| Mgi Id | MGI:2150474 | Doi | 10.1046/j.0019-2805.2001.01277.x |
| Citation | Bi B, et al. (2001) Cleavage of E2F-1-regulating proteins and activation of E2F-1 during CD95-induced death of thymocytes. Immunology 104(1):37-42 |
| abstractText | The CD95 death receptor activates caspases that cleave a variety of intracellular substrates, including cell cycle control proteins. However, the significance of this cleavage for the induction of apoptosis is unclear. In this study, CD95-induced cleavage of the G1/S checkpoint regulator proteins, retinoblastoma protein (pRb) and murine-double-minute-2 (mdm-2), was associated with an increased protein concentration of a key transcription factor, E2F-1, which is regulated by both of them. Furthermore, DNA-binding activity to E2F sites is increased. In thymocytes, CD95-induced apoptosis was associated with increased E2F-1 DNA-binding activity, while thymocytes that lacked E2F-1 were less susceptible to CD95-induced apoptosis. We conclude that the G1/S checkpoint is an important target of CD95 signalling. CD95-activated caspases cleave regulator proteins to increase E2F-1 activity, and inappropriate activation of E2F-1 is part of the mechanism of CD95-induced apoptosis. |
