HDAC3 influences phosphorylation of STAT3 at serine 727 by interacting with PP2A
| Autor: | Asuka Nanbo, Osamu Ikeda, Tadashi Matsuda, Shinya Kamitani, Shiho Kawakami, Sumihito Togi, Ryuta Muromoto |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2009 |
| Předmět: |
STAT3 Transcription Factor
Transcriptional Activation Biophysics Hydroxamic Acids Biochemistry Histone Deacetylases STAT3 Sp3 transcription factor Genes Reporter medicine Serine Humans transcriptional regulation Protein Phosphatase 2 Enzyme Inhibitors Phosphorylation RNA Small Interfering Luciferases Molecular Biology Histone deacetylase 5 biology HDAC3 Cell Biology Protein phosphatase 2 Molecular biology dephosphorylation PP2A Histone Deacetylase Inhibitors Trichostatin A biology.protein Histone deacetylase Leukemia inhibitory factor medicine.drug HeLa Cells Signal Transduction |
| Zdroj: | Biochemical and Biophysical Research Communications. 379(2):616-620 |
| ISSN: | 0006-291X |
| Popis: | Signal transducer and activator of transcription 3 (STAT3), which mediates biological actions in many physiological processes, is activated by cytokines and growth factors, and has been reported to be involved in the pathogenesis of various human diseases. Here, we show that treatment of HeLa cells with a histone deacetylase (HDAC) inhibitor, trichostatin A, or small-interfering RNA (siRNA)-mediated repression of HDAC3, enhances phosphorylation of STAT3 at Ser727. Furthermore, dephosphorylation of STAT3 at Ser727 by protein phosphatase 2A (PP2A) was restored by treatment of cells with HDAC3 siRNA. We further found that formation of a complex between STAT3 and PP2A was enhanced in the presence of HDAC3. Importantly, small-interfering RNA-mediated repression of both HDAC3 and PP2A effectively enhanced leukemia inhibitory factor (LIF)-induced STAT3 activation. These results indicate that HDAC3 may act as a scaffold protein for PP2A to regulate the LIF/STAT3-mediated signaling pathway. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect