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Stat3 Dimerization Regulated by Reversible Acetylation of a Single Lysine Residue

2005/01/13 by Zheng-long Yuan, Zhenglong Yuan, Ying-jie Guan +3 · 29 citations
Medicine · Biochemistry, Genetics and Molecular Biology · #Cytokine Signaling Pathways and Interactions #NF-κB Signaling Pathways #Genomics, phytochemicals, and oxidative stress

paper · doi:10.1126/science.1105166

Abstract

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.

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