| First Author | Morimoto H | Year | 2007 |
| Journal | J Biol Chem | Volume | 282 |
| Issue | 49 | Pages | 35449-56 |
| PubMed ID | 17928297 | Mgi Jnum | J:129006 |
| Mgi Id | MGI:3768486 | Doi | 10.1074/jbc.M704079200 |
| Citation | Morimoto H, et al. (2007) Activation of a C-terminal transcriptional activation domain of ERK5 by autophosphorylation. J Biol Chem 282(49):35449-56 |
| abstractText | ERK5 plays a crucial role in many biological processes by regulating transcription. ERK5 has a large C-terminal-half that contains a transcriptional activation domain. However, it has remained unclear how its transcriptional activation activity is regulated. Here, we show that the activated kinase activity of ERK5 is required for the C-terminal-half to enhance the AP-1 activity, and that the activated ERK5 undergoes autophosphorylation on its most C-terminal region. Changing these phosphorylatable threonine and serine residues to unphosphorylatable alanines significantly reduces the transcriptional activation activity of ERK5. Moreover, phosphomimetic mutants of the C-terminal-half of ERK5 without an N-terminal kinase domain are shown to be able to enhance the AP-1 activity in fibroblastic cells. These results reveal the role of the stimulus-induced ERK5 autophosphorylation in regulation of gene expression. |
