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J Biol Chem, Vol. 273, Issue 44, 28625-28632, October 30, 1998
From the Department of Pharmacology, University of Texas
Southwestern Medical Center, Dallas, Texas 75235-9041
Several components of the budding yeast
pheromone-response pathway are conserved in mammalian mitogen-activated
protein (MAP) kinase pathways. Thus, we used degenerate
oligonucleotides derived from the sequence of the Saccharomyces
cerevisiae protein kinase Ste20p to amplify related sequences
from the rat. One of these sequences was used to clone a rat Ste20p
homolog, which we called TAO1 for its one thousand and one amino acids.
Northern analysis shows TAO1 is highly expressed in brain, as is a
homolog TAO2. Recombinant TAO1 was expressed and purified from
Sf9 cells. In vitro, it activated MAP/extracellular
signal-regulated protein kinase (ERK) kinases (MEKs) 3, 4, and 6 of the
stress-responsive MAP kinase pathways, but not MEK1 or 2 of the
classical MAP kinase pathway. TAO1 activated MEK3 but not MEK4 or MEK6
in transfected cells. MEK3 coimmunoprecipitated with TAO1 when they
were expressed in 293 cells. In addition, immunoreactive MEK3
endogenous to Sf9 cells copurified with TAO1 produced from a
recombinant baculovirus. The activation of and binding to MEK3 by TAO1
implicates TAO1 in the regulation of the p38-containing
stress-responsive MAP kinase pathway.
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