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

Science (New York, N.Y.) | Jan 14, 2005

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 RIS Download

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

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