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J. Biol. Chem., Vol. 269, Issue 48, 30089-30092, Dec, 1994
CC Li, RM Dai, E Chen and DL Longo
We have previously shown that NF-kappa B/Rel family members are physically
associated phosphoproteins, and p105 and p50 are hyperphosphorylated after
NF-kappa B activation. In this report, we further studied the
phosphorylation involved in NF-kappa B activation in Jurkat T cells
responding to phorbol 12-myristate 13-acetate and phytohemagglutinin.
Immediately following stimulation, p50 is hyperphosphorylated, and a
phosphorylated form of p50 (pp50) is translocated from the cytoplasm to the
nucleus. The kinetics of this nuclear translocation paralleled that of the
appearance of an active kappa B DNA-binding complex. An at least 30-fold
higher level of kappa B DNA binding was detected in pp50 than p50. The
enhanced binding could be attributed to a much greater stability detected
in the complex consisting of kappa B DNA and pp50, but not p50. These
results suggest that phosphorylation of p50, and perhaps other family
members as well, may be involved in the activation of NF-kappa B/Rel family
transcription factors.
Phosphorylation of NF-KB1-p50 is involved in NF-kappa B activation and stable DNA binding
Biological Carcinogenesis and Development Program, Program Resources, Inc./Dyncorp, Frederick, Maryland.
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