期刊
SCIENCE
卷 306, 期 5694, 页码 271-275出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1099414
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资金
- NIAID NIH HHS [AI43477, R21AI48542] Funding Source: Medline
- NIEHS NIH HHS [ES04151, ES06376] Funding Source: Medline
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.
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