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Regulation of STAT signaling by acetylation

Shougang Zhuang1

  • 1Department of Nephrology, Shanghai East Hospital, Tongji University School of Medicine, Shanghai 200120, China. szhuang@lifespan.org

Cellular Signalling
|May 28, 2013
PubMed

Insights

Signal transducers and activators of transcription (STATs) are activated by JAK kinases. STAT acetylation, regulated by HATs and HDACs, modulates STAT activation and gene expression.

Area of Science:

  • Molecular Biology
  • Cellular Signaling
  • Gene Regulation

Background:

  • Signal transducers and activators of transcription (STATs) are latent cytoplasmic factors activated by tyrosine phosphorylation.
  • Activation involves JAK tyrosine kinases responding to cytokines and growth factors.
  • Activated STATs dimerize, translocate to the nucleus, and induce gene expression.

Purpose of the Study:

  • To review the characterization of STAT acetylation.
  • To highlight the role of acetylation in modulating STAT activation.

Main Methods:

  • Review of existing literature on STAT acetylation.
  • Analysis of the interplay between histone acetyltransferases (HATs) and histone deacetylases (HDACs) in STAT modification.

Main Results:

  • Acetylation has been identified in multiple STAT proteins, including STAT1, STAT2, STAT3, STAT5b, and STAT6.
  • STAT acetylation is dependent on the balance between HATs (e.g., CBP/p300) and HDACs.

Conclusions:

  • STAT acetylation is a critical post-translational modification.
  • Acetylation influences STAT activity and downstream gene regulation, impacting cellular events.

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