| First Author | Gao M | Year | 2004 |
| Journal | Science | Volume | 306 |
| Issue | 5694 | Pages | 271-5 |
| PubMed ID | 15358865 | Mgi Jnum | J:93082 |
| Mgi Id | MGI:3055697 | Doi | 10.1126/science.1099414 |
| Citation | Gao M, et al. (2004) Jun turnover is controlled through JNK-dependent phosphorylation of the E3 ligase Itch. Science 306(5694):271-5 |
| abstractText | The turnover of Jun proteins, like that of other transcription factors, is regulated through ubiquitin-dependent proteolysis. Usually, such processes are regulated by extracellular stimuli through phosphorylation of the target protein, which allows recognition by F box-containing E3 ubiquitin ligases. In the case of c-Jun and JunB, we found that extracellular stimuli also modulate protein turnover by regulating the activity of an E3 ligase by means of its phosphorylation. Activation of the Jun amino-terminal kinase (JNK) mitogen-activated protein kinase cascade after T cell stimulation accelerated degradation of c-Jun and JunB through phosphorylation-dependent activation of the E3 ligase Itch. This pathway modulates cytokine production by effector T cells. |
