| First Author | Li Y | Year | 2017 |
| Journal | FEBS Lett | Volume | 591 |
| Issue | 18 | Pages | 2859-2868 |
| PubMed ID | 28777872 | Mgi Jnum | J:266112 |
| Mgi Id | MGI:6212886 | Doi | 10.1002/1873-3468.12779 |
| Citation | Li Y, et al. (2017) The short isoform of PML-RARalpha activates the NRF2/HO-1 pathway through a direct interaction with NRF2. FEBS Lett 591(18):2859-2868 |
| abstractText | The NF-E2 p45-related factor 2 (NRF2)-Kelch-like ECH-associated protein 1 signaling pathway plays an important role in cytoprotection. In acute promyelocytic leukemia, fusion of the promyelocytic leukemia protein (PML) with retinoic acid receptor alpha (RARalpha) results in an oncogene, PML-RARalpha (PR). Although previous studies have shown that both RARalpha and PML inhibit NRF2 activity, how PR regulates NRF2 has not been reported. Here, we discovered that PR-S, the short isoform of PR, potentiates NRF2 activity in a tert-butylhydroquinone (tBHQ) concentration-dependent manner. Furthermore, PR-S colocalized with NRF2 in HeLa and HEK293T cells. The association of PR-S and NRF2 is mediated by the DNA-binding domains of RARalpha and the Neh7 domain of NRF2. Our results define a novel function of PR-S as a NRF2-transcriptional co-activator. |
