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.
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
Science
Date: Jan. 14, 2005
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