Journal
COLD SPRING HARBOR PERSPECTIVES IN BIOLOGY
Volume 1, Issue 4, Pages -Publisher
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1101/cshperspect.a000067
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Funding
- National Institutes of Health (NIH), NIAID [K99CA137171]
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Nuclear factor-kappa B (NF-kappa B) is a pleiotropic mediator of inducible and specific gene regulation involving diverse biological activities including immune response, inflammation, cell proliferation, and death. The fine-tuning of the NF-kappa B DNA binding activity is essential for its fundamental function as a transcription factor. An increasing body of literature illustrates that this process can be elegantly and specifically controlled at multiple levels by different protein subsets. In particular, the recent identification of a non-Rel subunit of NF-kappa B itself provides a new way to understand the selective high-affinity DNA binding specificity of NF-kappa B conferred by a synergistic interaction within the whole complex. Here, we review the mechanism of the specification of DNA binding activity of NF-kappa B complexes, one of the most important aspects of NF-kappa B transcriptional control.
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