| First Author | Ochocka AM | Year | 2009 |
| Journal | FEBS Lett | Volume | 583 |
| Issue | 4 | Pages | 621-6 |
| PubMed ID | 19166840 | Mgi Jnum | J:201310 |
| Mgi Id | MGI:5512955 | Doi | 10.1016/j.febslet.2009.01.009 |
| Citation | Ochocka AM, et al. (2009) FKBP25, a novel regulator of the p53 pathway, induces the degradation of MDM2 and activation of p53. FEBS Lett 583(4):621-6 |
| abstractText | The p53 tumour suppressor protein is tightly controlled by the E3 ubiquitin ligase, mouse double minute 2 (MDM2), but maintains MDM2 expression as part of a negative feedback loop. We have identified the immunophilin, 25kDa FK506-binding protein (FKBP25), previously shown to be regulated by p53-mediated repression, as an MDM2-interacting partner. We show that FKBP25 stimulates auto-ubiquitylation and proteasomal degradation of MDM2, leading to the induction of p53. Depletion of FKBP25 by siRNA leads to increased levels of MDM2 and a corresponding reduction in p53 and p21 levels. These data are consistent with the idea that FKBP25 contributes to regulation of the p53-MDM2 negative feedback loop. |
