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

Norihiko Ohbayashi1, Osamu Ikeda, Naohisa Taira

  • 1Department of Immunology, Graduate School of Pharmaceutical Sciences Hokkaido University, Kita-ku, Sapporo, Japan.

Biological & Pharmaceutical Bulletin
|October 6, 2007
PubMed

Insights

Leukemia inhibitory factor (LIF) and interleukin-6 (IL-6) activate signal transducer and activator of transcription 3 (STAT3) through acetylation at Lys-685, mediated by the PI3K/Akt pathway.

Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Biochemistry

Background:

  • Signal transducer and activator of transcription 3 (STAT3) regulates numerous physiological processes.
  • STAT3 activation involves phosphorylation, dimerization, and nuclear translocation.
  • Previous research identified Lys-685 acetylation by p300 as critical for STAT3 activation.

Purpose of the Study:

  • To investigate the role of STAT3 acetylation at Lys-685 in response to specific cytokines.
  • To elucidate the signaling pathway involved in STAT3 Lys-685 acetylation.

Main Methods:

  • Development of an antibody specific to acetylated STAT3 at Lys-685.
  • Treatment of 293T and Hep3B cells with leukemia inhibitory factor (LIF) or interleukin-6 (IL-6).
  • Inhibition of the PI3K/Akt pathway using LY294002 or a dominant-negative Akt mutant.

Main Results:

  • LIF and IL-6 induced STAT3 acetylation at Lys-685 in treated cells.
  • STAT3 Lys-685 acetylation was significantly reduced by PI3K/Akt pathway inhibitors.
  • Endogenous STAT3 acetylation at Lys-685 is confirmed to be regulated by LIF/IL-6 via PI3K/Akt.

Conclusions:

  • STAT3 acetylation at Lys-685 is a key regulatory event induced by LIF and IL-6.
  • The PI3K/Akt signaling pathway is essential for mediating STAT3 Lys-685 acetylation.
  • This study provides novel insights into the post-translational modification and activation of STAT3.

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