Nuclear factor B (NF-B) encompasses an important family of inducible transcriptional activators that regulate a wide variety of cellular and viral genes (1). The family members include p50, p52, p65 (RelA), c-Rel, and RelB. (2). The p65 subunit, similar to two others in the B family, RelB and c-Rel, contains two transactivation domains in the C-terminal region of the protein (3). Association with inhibitory proteins of the I?B family retains NF-?B in the cytoplasm. Degradation of IB proteins exposes the nuclear localization sequence (NLS), leading to nuclear translocation and subsequent binding of NF-B to DNA (4). p65 phosphorylation events occur in the cytoplasm or in the nucleus and are stimuli-specific and cell-type specific, on serine 276, 529, and 536 by various kinases, such as PKA, casein kinase II, IKK beta, and RSK1. Phosphorylation on these sites has been linked to regulation of NF-?B activation (5).
Related Pathway
Apoptosis
Delta-Notch Signaling Pathway
MAPK signaling pathway
Toll-like receptor signaling pathway
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Western blot analysis on Daudi cell lysates using anti-Phospho-NF-kappa-B (pS536), 1:20,000 dilution. Cells were either (A) untreated (B) treated with Calyculin A + TNF-alpha
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