期刊
NATURE COMMUNICATIONS
卷 4, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms2916
关键词
-
资金
- American Cancer Society [RSG-13-052-01-MPC]
- National Institutes of Health [R00CA137171, T32CA009110]
CD25, the alpha chain of the interleukin-2 receptor, is expressed in activated T cells and has a significant role in autoimmune disease and tumorigenesis; however, the mechanisms regulating transcription of CD25 remain elusive. Here we identify the Src-associated substrate during mitosis of 68 kDa (Sam68) as a novel non-Rel component in the nuclear factor-kappaB (NF-kappa B) complex that confers CD25 transcription. Our results demonstrate that Sam68 has an essential role in the induction and maintenance of CD25 in T cells. T-cell receptor engagement triggers translocation of the inhibitor of NF-kappa B kinase alpha (IKK alpha) from the cytoplasm to the nucleus, where it phosphorylates Sam68, causing complex formation with NF-kappa B in the nucleus. These findings reveal the important roles of KH domain-containing components and their spatial interactions with IKKs in determining the binding targets of NF-kappa B complexes, thus shedding novel insights into the regulatory specificity of NF-kappa B.
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