دورية أكاديمية
Phosphorylation-dependent Regulation of Stability and Transforming Potential of ETS Transcriptional Factor ESE-1 by p21-activated Kinase 1.
| العنوان: | Phosphorylation-dependent Regulation of Stability and Transforming Potential of ETS Transcriptional Factor ESE-1 by p21-activated Kinase 1. |
|---|---|
| المؤلفون: | Manavathi, Bramanandam1, Rayala, Suresh K.1, Kumar, Rakesh1,2 rkumar@mdanderson.org. |
| المصدر: | Journal of Biological Chemistry. 7/6/2007, Vol. 282 Issue 27, p19820-19830. 11p. 9 Graphs. |
| مصطلحات موضوعية: | *PHOSPHORYLATION, *TRANSCRIPTION factors, *EPITHELIUM, *MICROBIAL genetics, *GENE expression, *EPITHELIAL cells, *CANCER cells |
| مستخلص: | Differential phosphorylation of transcription factors by signal transduction pathways play an important role in regulation of gene expression and functions. ESE-1 is an epithelium-specific ETS transcription factor that transforms human breast epithelial cells through a serine- and aspartic acid-rich domain (SAR) by an unknown cytoplasmic mechanism. Here we found that a signaling kinase, p21-activated kinase-1 (Pak1), interacts with and phosphorylates ESE-1. Interestingly, Pak1 selectively phosphorylates ESE-1 at Ser207, which is located within the SAR domain. A S207A substitution in ESE-1 reduced its ability to transform breast cancer cells. We also found that ESE-1 is a labile protein and by interacting with F-box-binding protein β-TrCP, undergoes ubiquitin-dependent proteolysis. Intriguingly, Pak1 phosphorylation inactive mutant ESE1-S207A is more unstable than either wild-type ESE-1 or its Pak1 phosphorylation mimetic mutant, i.e. ESE1-S207E. These findings provide novel insights into the mechanism of transformation potential of ESE-1 and discovered that ESE-1 functions are coordinately regulated by Pak1 phosphorylation and β-TrCP-dependent ubiquitin-proteasome pathways. [ABSTRACT FROM AUTHOR] |
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