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MBC in Press, published online ahead of print September 24, 2002
Mol. Biol. Cell 10.1091/mbc.E02-03-0149

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Submitted on March 18, 2002
Revised on August 15, 2002
Accepted on September 4, 2002

Calcium regulation of GM-CSF by calmodulin dependent kinase II phosphorylation of Ets1

Hebin Liu1 and Thomas Grundström1*

1 Department of Molecular Biology, Umeå University, S-901 87 Umeå, Sweden

* Corresponding author. E-mail address: Thomas.Grundstrom{at}molbiol.umu.se.

The multipotent cytokine granulocyte macrophage-colony stimulating factor (GM-CSF) is in particular involved in the physiological response to infection and in inflammatory responses. GM-CSF is produced by many cell types including T lymphocytes responding to T cell receptor (TCR) activation and mantle zone B lymphocytes. B cell receptor (BCR) and TCR activation generates two major signals; an increase in intracellular Ca2+ concentration and a protein kinase cascade. Previous studies have shown that the Ca2+/calmodulin dependent phosphatase calcineurin mediates stimulation of GM-CSF transcription in response to Ca2+. In this study, we show that Ca2+ signaling also regulates GM-CSF transcription negatively through Ca2+/calmodulin dependent kinase II (CaMK II) phosphorylation of serines in the auto-inhibitory domain for DNA binding of the transcription factor Ets1. Wild type Ets1 negatively affects GM-CSF transcription upon Ca2+ stimulation in the presence of cyclosporin A, which inhibits calcineurin. Conversely, Ets1 with mutated CaMK II target serines showed an increase in transactivation of the GM-CSF promoter/enhancer. Moreover, constitutively active CaMK II inhibited transactivation of GM-CSF by wild type Ets1 but not by Ets1 with mutated CaMK II sites. Mutation of CaMK II target serines in Ets1 also relieves inhibition of co-operative transactivation of GM-CSF with the Runx1/AML1 transcription factor. In addition, the Ca2+ dependent phosphorylation of Ets1 reduces the binding of Ets1 to the GM-CSF promoter in vivo.




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