LIF- and IL-6-induced acetylation of STAT3 at Lys-685 through PI3K/Akt activation - PubMed (original) (raw)

. 2007 Oct;30(10):1860-4.

doi: 10.1248/bpb.30.1860.

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LIF- and IL-6-induced acetylation of STAT3 at Lys-685 through PI3K/Akt activation

Norihiko Ohbayashi et al. Biol Pharm Bull. 2007 Oct.

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Abstract

Signal transducer and activator of transcription 3 (STAT3), which mediates biological actions in many physiological processes, is activated by cytokines and growth factors via specific tyrosine or serine phosphorylation, dimerization and nuclear translocation. A recent study has demonstrated, by using antibody to acetylated lysine, and a STAT3 mutant with Lys-685-to-Arg substitution, that STAT3 is acetylated at Lys-685 by histone acetyltransferase p300, and that acetylation at Lys-685 is critical for STAT3 activation. In the present study, we created an acetyl-specific antibody against STAT3 acetylated at Lys-685, and found that leukemia inhibitory factor (LIF) or interleukin (IL)-6 induced acetylation of STAT3 at Lys-685 in 293T and Hep3B cells. Moreover, acetylation of STAT3 at Lys-685 was suppressed by PI3K inhibitor LY294002, or a dominant negative Akt. Taken together, our findings demonstrate that endogenous STAT3 is acetylated at Lys-685 by LIF or IL-6 through PI3K/Akt activation.

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