Phosphorylation of Sp1 enhances HDAC1 recruitment to inhibit RECK expression
| Autor: | Kun-jing Hong, 洪琨景 |
|---|---|
| Rok vydání: | 2008 |
| Druh dokumentu: | 學位論文 ; thesis |
| Popis: | 96 Transcription factor Sp1 regulates both negatively and positively the expression of target genes by interacting different co-activator or co-repressor. Our previous studies showed that Her2/neu oncogene inhibited RECK (reversion-inducing cysteine rich protein with Kazal motifs)transcription via the ERK/Sp1 signaling pathway and histone deacetylase (HDAC) inhibitor, trichostatin A(TSA), reversed expression of RECK and reduced cancer cell metastasis. Therefore, we purposed that RECK gene transcription activity was controlled by Sp1 and HDAC1 interaction. By GST pull-down assay, we discovered that zinc-finger DNA binding domain is a crucial site which affected Sp1 binding with HDAC1. Further investigation revealed that the phosphorylation at Thr739 residue of Sp1 regulated the level of RECK transcription as determined by co-immunoprecipitation、luciferase assay and RT-PCR. Based on these results, we suggest that phosphorylation at Thr739 of Sp1 by the ERK/Sp1 signaling pathway can recruit HDAC1 to inhibit RECK gene trancription. |
| Databáze: | Networked Digital Library of Theses & Dissertations |
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