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J Biol Chem, Vol. 274, Issue 43, 30353-30356, October 22, 1999
B Kinases Phosphorylate NF-B p65 Subunit on Serine 536 in the Transactivation Domain
From the Discovery Research Laboratory, Tanabe Seiyaku Co.,
Ltd., 16-89 Kashima 3-chome, Yodogawa-ku, Osaka 532-8505, Japan
Recent investigations have elucidated the
cytokine-induced NF-
B activation pathway. IB kinase (IKK)
phosphorylates inhibitors of NF-B (IBs). The phosphorylation
targets them for rapid degradation through a ubiquitin-proteasome
pathway, allowing the nuclear translocation of NF-B. We have
examined the possibility that IKK can phosphorylate the p65 NF-B
subunit as well as IB in the cytokine-induced NF-B activation. In
the cytoplasm of HeLa cells, the p65 subunit was rapidly phosphorylated
in response to TNF-
in a time dependent manner similar to IB
phosphorylation. In vitro phosphorylation with GST-fused
p65 showed that a p65 phosphorylating activity was present in the
cytoplasmic fraction and the target residue was Ser-536 in the
carboxyl-terminal transactivation domain. The endogenous IKK complex,
overexpressed IKKs, and recombinant IKK
efficiently phosphorylated
the same Ser residue of p65 in vitro. The major
phosphorylation site in vivo was also Ser-536. Furthermore, activation of IKKs by NF-B-inducing kinase induced phosphorylation of p65 in vivo. Our finding, together with previous
observations, suggests dual roles for IKK complex in the regulation of
NF-B·IB complex.
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