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Volume 270, Number 16, Issue of April 21, pp. 9169-9177, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
cAMP-dependent Protein Kinase Is Necessary for Increased NF-E2DNA Complex Formation during Erythroleukemia Cell Differentiation

Arlene D. Garingo , Modem Suhasini , Nancy C. Andrews , Renate B. Pilz

When murine erythroleukemia (MEL) cells are induced to differentiate by hexamethylene bisacetamide (HMBA), erythroid-specific genes are transcriptionally activated; however, transcriptional activation of these genes is severely impaired in cAMP-dependent protein kinase (protein kinase A)-deficient MEL cells. The transcription factor NF-E2, composed of a 45-kDa (p45) and an 18-kDa (p18) subunit, is essential for enhancer activity of the globin locus control regions (LCRs). DNA binding of NF-E2 and -globin LCR enhancer activity was significantly less in HMBA-treated protein kinase A-deficient cells compared to cells containing normal protein kinase A activity; DNA binding of several other transcription factors was the same in both cell types. In parental cells, HMBA treatment and/or prolonged activation of protein kinase A increased the amount of NF-E2DNA complexes without change in DNA binding affinity; the expression of p45 and p18 was the same under all conditions. p45 and p18 were phosphorylated by protein kinase A in vitro, but the phosphorylation did not affect NF-E2DNA complexes, suggesting that protein kinase A regulates NF-E2DNA complex formation indirectly, e.g. by altering expression of a regulatory factor(s). Thus, protein kinase A appears to be necessary for increased NF-E2DNA complex formation during differentiation of MEL cells and may influence erythroid-specific gene expression through this mechanism.



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