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

Norihiko Ohbayashi, Osamu Ikeda, Naohisa Taira, Yu Yamamoto, Ryuta Muromoto, Yuichi Sekine, Kenji Sugiyama, Tsutomu Honjoh, Tadashi Matsuda

    Research output: Contribution to journalArticlepeer-review

    41 Citations (Scopus)

    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.

    Original languageEnglish
    Pages (from-to)1860-1864
    Number of pages5
    JournalBiological and Pharmaceutical Bulletin
    Volume30
    Issue number10
    DOIs
    Publication statusPublished - 2007 Oct

    Keywords

    • Acetylation
    • Akt
    • Interleukin-6
    • Leukemia inhibitory factor
    • PI3K
    • Signal transducer and activator of transcription 3

    ASJC Scopus subject areas

    • Pharmacology
    • Pharmaceutical Science

    Fingerprint Dive into the research topics of 'LIF- and IL-6-induced acetylation of STAT3 at Lys-685 through PI3K/Akt activation'. Together they form a unique fingerprint.

    Cite this