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Stat3 dimerization regulated by reversible acetylation of a single lysine residue.

Upon cytokine treatment, members of the signal transducers and activators of transcription (STAT) family of proteins are phosphorylated on tyrosine and serine sites within the carboxyl-terminal region in cells. We show that in response to cytokine treatment, Stat3 is also acetylated on a single lysine residue, Lys685. Histone acetyltransferase p300-mediated Stat3 acetylation on Lys685 was reversible by type I histone deacetylase (HDAC). Use of a prostate cancer cell line (PC3) that lacks Stat3 and PC3 cells expressing wild-type Stat3 or a Stat3 mutant containing a Lys685-to-Arg substitution revealed that Lys685 acetylation was critical for Stat3 to form stable dimers required for cytokine-stimulated DNA binding and transcriptional regulation, to enhance transcription of cell growth-related genes, and to promote cell cycle progression in response to treatment with oncostatin M.

Pubmed ID: 15653507

Authors

  • Yuan ZL
  • Guan YJ
  • Chatterjee D
  • Chin YE

Journal

Science (New York, N.Y.)

Publication Data

January 14, 2005

Associated Grants

None

Mesh Terms

  • Acetylation
  • Acetyltransferases
  • Arginine
  • Cell Cycle
  • Cell Line, Tumor
  • Cell Nucleus
  • Cyclin D1
  • Cytokines
  • Cytoplasm
  • DNA
  • DNA-Binding Proteins
  • Dimerization
  • HeLa Cells
  • Histone Acetyltransferases
  • Histone Deacetylases
  • Humans
  • Interferon-alpha
  • Lysine
  • Mutation
  • Nuclear Proteins
  • Oncostatin M
  • Peptides
  • Phosphorylation
  • Protein Structure, Secondary
  • Proto-Oncogene Proteins c-bcl-2
  • Proto-Oncogene Proteins c-myc
  • Recombinant Fusion Proteins
  • STAT3 Transcription Factor
  • Signal Transduction
  • Trans-Activators
  • Transcriptional Activation
  • bcl-X Protein
  • src Homology Domains