Back to Search
Start Over
Dynamic modification of the ETS transcription factor PEA3 by sumoylation and p300-mediated acetylation
- Source :
- Nucleic Acids Research
- Publication Year :
- 2011
- Publisher :
- Oxford University Press, 2011.
-
Abstract
- Transcription factor activity is often controlled through the dynamic use of post-translational modifications. Two such modifications are acetylation and sumoylation, which both occur on lysine residues, providing the opportunity for cross-talk at the molecular level. Here, we focussed on the ETS-domain transcription factor PEA3 and studied the potential interplay between these two modifications. We demonstrate that PEA3 is acetylated in a p300-dependent manner. ERK MAPK pathway signalling potentiates acetylation of PEA3, and enhances its trans-activation capacity. However, the major acetylation and sumoylation events take place on the same sites in PEA3 making simultaneous modification impossible. Indeed, manipulation of either the sumoylation or acetylation pathways causes reciprocal changes in PEA3 acetylation and sumoylation respectively. However, despite the mutually exclusive nature of these modifications, both contribute to the trans-activation capacity of PEA3, implying that a dynamic series of modification events occurs during the activation process.
- Subjects :
- Protein sumoylation
Transcriptional Activation
Lysine
SUMO protein
P300-CBP Transcription Factors
Biology
Gene Regulation, Chromatin and Epigenetics
Cell Line
03 medical and health sciences
0302 clinical medicine
Genetics
Humans
p300-CBP Transcription Factors
Binding site
Transcription factor
030304 developmental biology
0303 health sciences
Binding Sites
ETS transcription factor family
Sumoylation
Acetylation
Cell biology
body regions
030220 oncology & carcinogenesis
Cancer research
Transcription Factors
Subjects
Details
- Language :
- English
- ISSN :
- 13624962 and 03051048
- Volume :
- 39
- Issue :
- 15
- Database :
- OpenAIRE
- Journal :
- Nucleic Acids Research
- Accession number :
- edsair.doi.dedup.....fc656b7d27ba16563d92895bf395bf58