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Target Gene Specificity of USF-1 Is Directed via p38-mediated Phosphorylation-dependent Acetylation.

Abstract : How transcription factors interpret the output from signal transduction pathways to drive distinct programs of gene expression is a key issue that underpins development and disease. The ubiquitously expressed basic-helix-loop-helix leucine zipper upstream stimulating factor-1 binds E-box regulatory elements (CANNTG) to regulate a wide number of gene networks. In particular, USF-1 is a key component of the tanning process. Following UV irradiation, USF-1 is phosphorylated by the p38 stress-activated kinase on threonine 153 and directly up-regulates expression of the POMC, MC1R, TYR, TYRP-1 and DCT genes. However, how phosphorylation on Thr-153 might affect the activity of USF-1 is unclear. Here we show that, in response to DNA damage, oxidative stress and cellular infection USF-1 is acetylated in a phospho-Thr-153-dependent fashion. Phospho-acetylated USF-1 is nuclear and interacts with DNA but displays altered gene regulatory properties. Phospho-acetylated USF-1 is thus proposed to be associated with loss of transcriptional activation properties toward several target genes implicated in pigmentation process and cell cycle regulation. The identification of this critical stress-dependent USF-1 modification gives new insights into understanding USF-1 gene expression modulation associated with cancer development.
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Contributor : Hervé De Villemeur Connect in order to contact the contributor
Submitted on : Thursday, July 16, 2009 - 10:32:42 AM
Last modification on : Wednesday, March 30, 2022 - 2:34:28 PM

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Sébastien Corre, Aline Primot, Yorann Baron, Jacques Le Seyec, Colin R. Goding, et al.. Target Gene Specificity of USF-1 Is Directed via p38-mediated Phosphorylation-dependent Acetylation.. Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2009, 284 (28), pp.18851-62. ⟨10.1074/jbc.M808605200⟩. ⟨inserm-00404297⟩



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