Salvat C, Aquaviva C, Jariel-Encontre I, Ferrara P, Pariat M, Steff A M, Carillo S, Piechaczyk M
Institut de Génétique Moléculaire, UMR5535 - CNRS, Montpellier, France.
Mol Biol Rep. 1999 Apr;26(1-2):45-51. doi: 10.1023/a:1006960021281.
The c-Fos and c-Jun oncoproteins and the p53 tumor suppressor protein are short-lived transcription factors. Several catabolic pathways contribute to their degradation in vivo. c-Fos and c-Jun are thus mostly degraded by the proteasome, but there is indirect evidence that, under certain experimental/physiological conditions, calpains participate in their destruction, at least to a limited extent. Lysosomes have also been reported to participate in the destruction of c-Fos. Along the same lines, p53 is mostly degraded following the ubiquitin/proteasome pathway and calpains also seem to participate in its degradation. Moreover, c-Fos, c-Jun and p53 turnovers are regulated upon activation of intracellular signalling cascades. All taken together, these observations underline the complexity of the mechanisms responsible for the selective destruction of proteins within cells.
原癌蛋白c-Fos和c-Jun以及肿瘤抑制蛋白p53是寿命较短的转录因子。几种分解代谢途径参与了它们在体内的降解过程。因此，c-Fos和c-Jun大多通过蛋白酶体降解，但有间接证据表明，在某些实验/生理条件下，钙蛋白酶至少在一定程度上参与了它们的破坏。也有报道称溶酶体参与了c-Fos的破坏。同样，p53大多在泛素/蛋白酶体途径后被降解，钙蛋白酶似乎也参与了其降解。此外，c-Fos、c-Jun和p53的周转在细胞内信号级联激活时受到调节。综上所述，这些观察结果突显了细胞内蛋白质选择性破坏机制的复杂性。
