Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are dual specificity protein phosphatases that specifically inactivate MAPKs. Regulated expression of MKPs plays a key role in determining their physiological function. However, little is known about the molecular mechanism of the activation of MKP genes. In this study, we cloned the rat MKP-2 gene and characterized its structure. The MKP-2 gene has four exons and three introns. The organization of exons of the MKP-2 gene is very similar to that of the MKP-1 gene, suggesting that MKP-1 and MKP-2 are derived from the same ancestral gene. We identified multiple transcription start sites (TSSs) for the MKP-2 gene. There is no functional TATA motif in the 5′ proximal region of the TSSs. Instead, this region is highly GC-rich and has two putative Sp1 sites. A 1.8 kb 5′ flanking region of the MKP-2 gene is sufficient to mediate transcriptional activation of the luciferase reporter gene by phorbol ester in GH3 cells. These results provide essential information about structural organization and regulatory sequences of the MKP-2 gene for further investigation of the molecular mechanisms of MKP-2 induction by extracellular stimuli.
|Number of pages||9|
|State||Published - Jul 25 2001|
Bibliographical noteFunding Information:
This work was supported by NIH grant HD34722 (to M.S.R.).
- Dual specificity protein phosphatase
- Mitogen-activated protein kinase
- TATA-less promoter
- Transcription start site
ASJC Scopus subject areas