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.
Highlights
Nuclear factor erythroid-derived 2 (NF-E2), a heterodimer comprised of a large tissue-specific p45 subunit and a small p18 Maf family subunit, plays an essential role in regulating multiple erythroid- and megakaryocytic-specific genes [1,2,3]
The p45/p18 heterodimer (NF-E2) has been reported to be modified by SUMO1 which lead to enhanced transcriptional activity of p45/NF-E2
NF-E2-DNA complex formation is increased by cAMP-dependent protein kinase A (PKA) [7,9]
Summary
Nuclear factor erythroid-derived 2 (NF-E2), a heterodimer comprised of a large tissue-specific p45 subunit and a small p18 Maf family subunit, plays an essential role in regulating multiple erythroid- and megakaryocytic-specific genes [1,2,3]. Murine erythroleukemia (MEL) cells lacking p45 show a reduction in globin gene expression, [4]. Patients with polycythemia vera disease (PV) present with elevated concentration of p45/NF-E2, overproduction of red cell and thrombocytopenia [6]. Tight control of NF-E2 activity is essential during erythroid differentiation. Post-translational modification has been shown to regulate NF-E2 transcriptional activity. CAMP-dependent protein kinase A (PKA) increases NF-E2/DNA complex formation in Murine erytholeukemia cell differentiation [7]. Small ubiquitin-like modifiers (SUMO) have been shown to exert control over NFE2 transcription [9]
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