Activation of the c-fos SRE through SAP-1a
| Autor: | H, Masutani, L, Magnaghi-Jaulin, S, Ait-Si-Ali, R, Groisman, P, Robin, A, Harel-Bellan, S, Ait Si Ali |
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| Rok vydání: | 1997 |
| Předmět: |
Serum Response Factor
Cancer Research genetic structures Response element Regulatory Sequences Nucleic Acid Biology Transfection PC12 Cells Transactivation Serum response factor Genetics Animals ets-Domain Protein Elk-4 Phosphorylation Molecular Biology Transcription factor Kinase Genes fos Nuclear Proteins Serum Response Element Recombinant Proteins eye diseases Rats Cell biology DNA-Binding Proteins Gene Expression Regulation Mitogen-activated protein kinase Calcium-Calmodulin-Dependent Protein Kinases biology.protein Binding domain |
| Zdroj: | Scopus-Elsevier |
| ISSN: | 1476-5594 0950-9232 |
| Popis: | TCFs, which are members of the Ets family of transcription factors, are recruited to the Serum Response Element (SRE) in the c-fos promoter by SRF. These Ets proteins, which are substrates for the MAP kinases, are direct targets of the Ras/MAP kinase signal transduction pathway. In this paper, we demonstrate that one of the TCFs, SAP-1a, displays a significant level of autonomous binding to the SRE Ets box. In contrast to previous observations, deletion of the SRF binding domain did not modulate the autonomous binding of SAP-1a. Also, the autonomous binding was not modulated by the phosphorylation of SAP-1a by MAP kinases. The autonomous binding was also detected in live cells: transfected SAP-1a was able to restore the response of a CArG-less SRE in PC12 cells. The response occurred in the absence of SRF recruitment since a mutant of SAP-1a in which the B-box, a domain required for interaction with SRF, had been deleted was still able to transactivate the CArG-less SRE. The transactivation was repressed by a Ras transdominant negative mutant, indicating the involvement of the Ras/MAP kinase pathway. Taken together, these data demonstrate that SAP-1a is capable of binding to the c-fos SRE in the absence of SRF. |
| Databáze: | OpenAIRE |
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