p38beta2-mediated phosphorylation and sumoylation of ATF7 are mutually exclusive
| Autor: | Mariel Donzeau, Claude Kedinger, Barbara Camuzeaux, Mustapha Oulad-Abdelghani, Bruno Chatton, Pierre-Jacques Hamard, Marc Vigneron, Jessica Diring |
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| Přispěvatelé: | Peney, Maité, Institut Gilbert-Laustriat : Biomolécules, Biotechnologie, Innovation Thérapeutique, Université Louis Pasteur - Strasbourg I-Centre National de la Recherche Scientifique (CNRS), Institut de génétique et biologie moléculaire et cellulaire (IGBMC), Université Louis Pasteur - Strasbourg I-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Louis Pasteur - Strasbourg I |
| Jazyk: | angličtina |
| Rok vydání: | 2008 |
| Předmět: |
Transcription
Genetic Response element SUMO protein Activating transcription factor Biology 03 medical and health sciences Mitogen-Activated Protein Kinase 11 Structural Biology MESH: Mitogen-Activated Protein Kinase 11 [SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular Biology [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Phosphorylation Protein kinase A Molecular Biology 030304 developmental biology 0303 health sciences General transcription factor MESH: Phosphorylation MESH: Transcription Genetic 030302 biochemistry & molecular biology Promoter Molecular biology Activating Transcription Factors Cell biology MESH: Activating Transcription Factors MESH: Small Ubiquitin-Related Modifier Proteins Small Ubiquitin-Related Modifier Proteins Transcription factor II D |
| Zdroj: | Journal of Molecular Biology Journal of Molecular Biology, 2008, 384 (4), pp.980-91. ⟨10.1016/j.jmb.2008.10.008⟩ Journal of Molecular Biology, Elsevier, 2008, 384 (4), pp.980-91. ⟨10.1016/j.jmb.2008.10.008⟩ |
| ISSN: | 0022-2836 1089-8638 |
| Popis: | International audience; The ubiquitous activating transcription factor (ATF) 7 binds as a homodimer to the cAMP response element/TPA response element motifs present in the promoters of its target genes. ATF7 is homologous to ATF2 and heterodimerizes with Jun or Fos proteins, modulating their DNA-binding specificities. We previously demonstrated that TAF12, a component of the TFIID general transcription factor, mediates ATF7 transcriptional activity through direct interactions between the two proteins. By contrast, ATF7, but not ATF2, is modified in vivo by sumoylation, which restricts its subcellular localization, thereby inhibiting its transcriptional activity. In the present study, we dissect the mechanism of this functional switch. We characterized the multisite phosphorylation of the ATF7 activation domain and identified one of the involved kinase, p38beta2 mitogen-activated protein kinase. In addition, we show that epidermal growth factor treatment results in a two-step modification mechanism of ATF7 activation domain. The Thr53 residue is phosphorylated first by a presently unknown kinase, allowing p38beta2 mitogen-activated protein kinase to modify the Thr51 residue, excluding the sumoylation of ATF7 protein. The resulting activation of transcription is related to an increased association of TAF12 with this phosphorylated form of ATF7. Our data therefore conclusively establish that sumoylation and phosphorylation of ATF7 are two antagonistic posttranslational modifications. |
| Databáze: | OpenAIRE |
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