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J Biol Chem, Vol. 274, Issue 7, 4096-4105, February 12, 1999
From the Cancer Research Campaign Centre for Cell and Molecular
Biology, Institute of Cancer Research, Chester Beatty Laboratories,
237 Fulham Rd., London SW3 6JB, United Kingdom
Hemopoietic cytokines such as interleukin-3 and
granulocyte colony-stimulating factor (G-CSF) are potent activators of
hemopoietic cell growth and strongly induce activation of extracellular
signal-regulated kinase (ERK), c-Jun-N-terminal kinase (JNK), and p38
mitogen-activated protein (MAP) kinases. However, the role of these
kinases is unclear. Using specific chemical inhibitors for MEK and p38,
we demonstrate here that both ERK and p38 pathways are critically
involved in the transduction of a proliferative signal and cooperate in
G-CSF-induced cell proliferation. We show that, like ERK and JNK
activation, activation of p38 and its downstream substrate MAP
kinase-activated protein kinase 2 by interleukin-3 or G-CSF requires
Ras activation. We demonstrate that two distinct cytoplasmic regions of
the G-CSF receptor are involved in activation of the p38 pathway: a
region within the 100 membrane-proximal amino acids is sufficient to induce low levels of p38 and MAP kinase-activated protein kinase 2 activation, whereas the membrane-distal phosphorylation site Tyr763 mediates strong activation of these kinases.
The levels of p38 activation correlate closely with those of Ras
activation by G-CSF, suggesting that the degree of Ras activation
is a critical determinant for the extent of p38 activation by
hemopoietic cytokines.
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