Abstract
Nuclear factor erythroid-derived 2 (NF-E2), a heterodimer composed of p45 and p18, is a transcriptional activator in hematopoietic progenitors. The transcriptional activity of NF-E2 is not only upregulated by SUMOylation but also stimulated by the cAMP-dependent protein kinase A (PKA). However, the relationship between SUMOylation and phosphorylation in the activation of NF-E2 is unclear. In the present studies, we have demonstrated that PKA enhances NF-E2 SUMOylation in an in vitro system using purified proteins, suggesting a possible mechanism for PKA-dependent activation of the NF-E2 transcription factor through SUMOylation.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphate / metabolism
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Cyclic AMP-Dependent Protein Kinases / metabolism
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Humans
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NF-E2 Transcription Factor / metabolism*
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Phosphorylation
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Sumoylation
Substances
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NF-E2 Transcription Factor
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Adenosine Triphosphate
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Cyclic AMP-Dependent Protein Kinases
Grants and funding
This work was supported by grants from the National Science Council in Taiwan (NSC98-2311-B-001-008-MY3) and Institute of Molecular Biology (to JH), Academia Sinica, National Science Council (
http://web1.nsc.gov.tw/mp.aspx?mp=7), and Institute of Molecular Biology (
http://www.imb.sinica.edu.tw/en/). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.