MKP-1 protein phosphatase participates in c-fos gene derepression in E1A and cHA-ras oncogene transformed fibroblasts under stress conditions
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- 作者：A. N. Kukushkin (1) (2)
S. B. Svetlikova (1) (2)
V. A. Pospelov (1) (2) - 关键词：MKP ; 1 ; c ; fos genes ; anisomycin ; transformed fibroblasts ; E1A ; cHa ; ras oncogenes
- 刊名：Cell and Tissue Biology
- 出版年：2014
- 出版时间：March 2014
- 年：2014
- 卷：8
- 期：2
- 页码：115-121
- 全文大小：791 KB
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S. B. Svetlikova (1) (2)
V. A. Pospelov (1) (2)
1. Institute of Cytology, Russian Academy of Sciences, St. Petersburg, Russia
2. St. Petersburg State University, St. Petersburg, Russia - ISSN：1990-5203
文摘
Immediate-early response gene c-fos expression is repressed and not activated after serum stimulation of serum-starved fibroblasts transformed with E1A and cHA-ras oncogenes. We found previously that stress factors, such as anisomycin, activated c-fos gene transcription in E1A+ras transformants. The MEK/ERK signal pathway played a primary role in this activation. In this paper, we investigated the role of MKP-1-dependent regulation of the c-fos gene through dephosphorylation of ERK kinases. It was revealed that anisomycin activated MKP-1 transcription in E1A+ras transformants for no longer than 1 h and then the transcriptional level dropped. Using MAP-kinase inhibitors, it was established that MKP-1 transcription depended on MEK/ERK and JNK kinase rather than p38 cascades. The anisomycin-induced c-fos gene transcription is stronger after the cell transfection with siRNA MKP-1. Thus, the MKP-1 protein phosphatase carries out negative regulation of c-fos gene transcription by dephosphorylation of ERK kinases, which are key signal components in E1A+ras-transformed cells exposed to the stress agent anisomycin.