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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Activation of a C-terminal transcriptional activation domain of ERK5 by autophosphorylation.

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.[1]


  1. Activation of a C-terminal transcriptional activation domain of ERK5 by autophosphorylation. Morimoto, H., Kondoh, K., Nishimoto, S., Terasawa, K., Nishida, E. J. Biol. Chem. (2007) [Pubmed]
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