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Activation of Stat3 sequence-specific DNA binding and transcription by p300/CREB-binding protein-mediated acetylation

Rui Wang1, Pratima Cherukuri, Jianyuan Luo

  • 1Department of Cancer Biology, University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA.

The Journal of Biological Chemistry
|January 15, 2005
PubMed

Insights

Signal transducer and activator of transcription 3 (Stat3) acetylation, mediated by p300/CREB-binding protein (CBP), enhances its DNA binding and activation. Inhibiting histone deacetylase increases Stat3 nuclear localization, revealing a new activation pathway.

Area of Science:

  • Cellular signaling and gene regulation
  • Molecular biology
  • Biochemistry

Background:

  • Signal transducers and activators of transcription (Stat) are cytoplasmic factors activated by tyrosine phosphorylation.
  • Activated Stats dimerize, translocate to the nucleus, and induce gene expression for cellular functions.

Purpose of the Study:

  • To investigate the post-translational modification of Stat3 by acetylation.
  • To identify the specific site and mechanism of Stat3 acetylation.
  • To determine the functional consequences of Stat3 acetylation on its activity.

Main Methods:

  • In vivo and in vitro acetylation assays.
  • Identification of acetylation sites using mass spectrometry.
  • Assays for DNA binding and transcriptional activation.
  • Histone deacetylase inhibition studies.

Main Results:

  • Stat3 is acetylated in vivo and in vitro.
  • Lysine 685 in the C-terminal domain is a major acetylation site, targeted by p300/CREB-binding protein (CBP).
  • Acetylation enhances Stat3's DNA binding and transactivation activity.
  • Histone deacetylase inhibition increases nuclear localization of Stat3.

Conclusions:

  • Stat3 undergoes acetylation, a novel post-translational modification.
  • Acetylation at Lysine 685 by p300/CBP positively regulates Stat3 activity.
  • This acetylation-dependent mechanism provides a new pathway for Stat3 activation in mammalian cells.

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