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J Biol Chem, Vol. 273, Issue 35, 22848-22855, August 28, 1998
,
From the Institut für Klinische Molekularbiologie und
Tumorgenetik der GSF, Marchioninistraße 25, D-81377 Munich, Germany
Raf kinases are regulators of cellular
proliferation, transformation, differentiation, and apoptosis. To
identify downstream targets of Raf-1 in vivo, we used NIH
3T3 fibroblasts expressing a Raf-1 kinase domain-estrogen receptor
fusion protein (BXB-ER), whose activity can be acutely regulated by
estrogen. Proteins differentially phosphorylated 20 min after BXB-ER
activation in living cells were displayed by two-dimensional
electrophoresis. The protein with the most prominent newly induced
phosphorylation was identified as stathmin, a phosphorylation-sensitive
regulator of microtubule dynamics. Stathmin is rapidly phosphorylated
on two ERK phosphorylation sites (serines 25 and 38) upon BXB-ER activation. The mitogen-activated protein kinase/extracellular signal-regulated kinase-kinase (MEK) inhibitor PD98059 abolished this
phosphorylation, demonstrating that stathmin is targeted by BXB-ER via
the MEK/ERK pathway. Prolonged BXB-ER activation resulted in the
accumulation of a stathmin phosphoisomer with impaired
microtubule-destabilizing activity. The appearance of this
phosphoisomer after BXB-ER activation correlated with rearrangements in
the microtubule network, resulting in the formation of long bundled
microtubules extending toward the rim of the cells. Our results
identify stathmin as a main target of the Raf/MEK/ERK kinase cascade
in vivo and strongly suggest that ERK-mediated stathmin
phosphorylation plays an important role for the microtubule reorganization induced by acute activation of Raf-1.
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