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Jun turnover is controlled through JNK-dependent phosphorylation of the E3 ligase Itch.
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| Author |
Gao, Min, et al. |
| Citation Information |
Science, 306: 271-5 (2004), : (2004) |
| Related Products |
AB10050 |
| Pub Med ID |
15358865 |
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Abstract
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.
