Target gene specificity of USF-1 is directed via p38-mediated phosphorylation-dependent acetylation.
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...
| Main Authors: | , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2009
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| _version_ | 1826270997796356096 |
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| author | Corre, S Primot, A Baron, Y Le Seyec, J Goding, C Galibert, MD |
| author_facet | Corre, S Primot, A Baron, Y Le Seyec, J Goding, C Galibert, MD |
| author_sort | Corre, S |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-06T21:49:40Z |
| format | Journal article |
| id | oxford-uuid:4ad0e832-d7d3-4c16-b884-a0383db3d9e8 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T21:49:40Z |
| publishDate | 2009 |
| record_format | dspace |
| spelling | oxford-uuid:4ad0e832-d7d3-4c16-b884-a0383db3d9e82022-03-26T15:39:48ZTarget gene specificity of USF-1 is directed via p38-mediated phosphorylation-dependent acetylation.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:4ad0e832-d7d3-4c16-b884-a0383db3d9e8EnglishSymplectic Elements at Oxford2009Corre, SPrimot, ABaron, YLe Seyec, JGoding, CGalibert, MDHow 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. |
| spellingShingle | Corre, S Primot, A Baron, Y Le Seyec, J Goding, C Galibert, MD Target gene specificity of USF-1 is directed via p38-mediated phosphorylation-dependent acetylation. |
| title | Target gene specificity of USF-1 is directed via p38-mediated phosphorylation-dependent acetylation. |
| title_full | Target gene specificity of USF-1 is directed via p38-mediated phosphorylation-dependent acetylation. |
| title_fullStr | Target gene specificity of USF-1 is directed via p38-mediated phosphorylation-dependent acetylation. |
| title_full_unstemmed | Target gene specificity of USF-1 is directed via p38-mediated phosphorylation-dependent acetylation. |
| title_short | Target gene specificity of USF-1 is directed via p38-mediated phosphorylation-dependent acetylation. |
| title_sort | target gene specificity of usf 1 is directed via p38 mediated phosphorylation dependent acetylation |
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