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J Biol Chem, Vol. 273, Issue 45, 29411-29416, November 6, 1998
B-dependent
Transcription by Tumor Necrosis Factor-
Is Mediated through
Phosphorylation of RelA/p65 on Serine 529
From the Lineberger Comprehensive Cancer Center and Department of
Biology, CB 7295, University of North Carolina, Chapel Hill,
North Carolina 27599-7295
Nuclear factor-
B (NF-B) is an essential
transcription factor in the control of expression of genes involved in
immune and inflammatory responses. In unstimulated cells, NF-B
complexes are sequestered in the cytoplasm through interactions with
IB
and other IB proteins. Extracellular stimuli that activate
NF-B, such as tumor necrosis factor (TNF), cause rapid
phosphorylation of IB at serines 32 and 36. The inducible
phosphorylation of IB is followed by its ubiquitination and
degradation, allowing NF-B complexes to translocate into the nucleus
and to activate gene expression. Previously, it has been shown that
TNF as well as other stimuli also lead to the phosphorylation of the
RelA/p65 subunit of NF-B. In this report, we demonstrate that the
TNF-induced phosphorylation of the RelA/p65 subunit occurs on serine
529, which is in the C-terminal (TA1) transactivation domain.
Accordingly, the TNF-induced phosphorylation of Rel/p65 increases
NF-B transcriptional activity but does not affect nuclear
translocation or DNA binding affinity.
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