Activation of a C-terminal transcriptional activation domain of ERK5 by autophosphorylation.
J Biol Chem
; 282(49): 35449-56, 2007 Dec 07.
Article
in En
| MEDLINE
| ID: mdl-17928297
ABSTRACT
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.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Transcription, Genetic
/
Gene Expression Regulation
/
Mitogen-Activated Protein Kinase 7
/
Fibroblasts
Limits:
Animals
Language:
En
Journal:
J Biol Chem
Year:
2007
Document type:
Article
Affiliation country:
Japan