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Blood, Vol. 95 No. 8 (April 15), 2000:
pp. 2552-2558
Granulocyte-macrophage colony-stimulating factor stimulation
results in phosphorylation of cAMP response
element-binding protein through activation of pp90RSK
Evelyn M. Kwon,
Maribeth A. Raines,
John Blenis, and
Kathleen M. Sakamoto
From the Division of Hematology-Oncology, Department of Pediatrics
and Department of Pathology & Laboratory Medicine, Gwynne Hazen Cherry
Memorial Laboratories, UCLA School of Medicine and Jonsson
Comprehensive Cancer Center, and the Department of Radiation Oncology,
UCLA School of Medicine, Los Angeles, CA; and the Department of Cell
Biology, Harvard Medical School, Boston, MA.
Granulocyte-macrophage colony-stimulating factor (GM-CSF) activates
several kinases and transcription factors through interaction with a
heterodimeric receptor complex. We previously demonstrated that
phosphorylation of the cyclic adenosine monophosphate (cAMP) response
element-binding protein, CREB, occurs through a protein kinase
A-independent pathway and is required for GM-CSF-induced transcriptional activation of the immediate early gene, early growth
response-1 (egr-1). Recent reports indicate that receptor tyrosine kinases can induce CREB phosphorylation through activation of
pp90RSK. We performed immune complex kinase assays in the human myeloid
leukemic cell line, TF-1, which revealed that GM-CSF induced pp90RSK
activation and phosphorylation of CREB within 5 minutes of stimulation.
Transfection with the kinase-defective pp90RSK expression plasmid
demonstrated a statistically significant decrease in transcriptional
activation of a  116 CAT/egr-1 promoter construct in response
to GM-CSF. Furthermore, activation of pp90RSK, CREB and egr-1
in GM-CSF-treated cells was inhibited by the presence of the
inhibitor, PD98059. In this study, we report that GM-CSF induces CREB
phosphorylation and egr-1 transcription by activating pp90RSK
through an MEK-dependent signaling pathway.
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