| First Author | He H | Year | 1998 |
| Journal | J Biol Chem | Volume | 273 |
| Issue | 39 | Pages | 25015-9 |
| PubMed ID | 9737957 | Mgi Jnum | J:50419 |
| Mgi Id | MGI:1303326 | Doi | 10.1074/jbc.273.39.25015 |
| Citation | He H, et al. (1998) c-Fos degradation by the proteasome. An early, Bcl-2-regulated step in apoptosis. J Biol Chem 273(39):25015-9 |
| abstractText | c-Fos is a transcription factor that promotes cell growth, differentiation, and transformation. We found that c-Fos was degraded when WEHI7.2 mouse lymphoma cells were induced to undergo apoptosis with the calcium ATPase inhibitor, thapsigargin, or the glucocorticoid hormone, dexamethasone. The degradation of c-Fos preceded caspase-3 activation and apoptotic nuclear chromatin condensation and was inhibited by the proteasome inhibitors MG132, N-acetyl-leucyl-leucyl-norleucinal, and lactacystin. Stable transfection of WEHI7.2 cells with a mutant form of c-Fos that was not degraded by the proteasome inhibited apoptosis. Also, overexpression of Bcl-2 in WEHI7.2 cells blocked c-Fos degradation and inhibited apoptosis. The results indicate that proteasome-mediated degradation of c-Fos is an early, Bcl-2-regulated step in apoptosis induction by thapsigargin and dexamethasone. These findings suggest that c-Fos may have a protective action that is eliminated by proteasome-mediated degradation and preserved by Bcl-2. |
