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Fig. 3.
Ras utilizes Raf-independent pathways to
up-regulate cyclin-associated kinase activity in RIE-1 cells.
A, exponentially growing cells stably expressing each DNA
were harvested, and cyclin D1-associated kinase assays were performed.
Cyclin D1 was immunoprecipitated, phosphorylation of recombinant GST-Rb
fusion protein was measured by an in vitro kinase assay, and
phosphorylation was quantitated using PhosphorImager analyses.
B, Ras utilizes Raf-independent pathways to up-regulate
cyclin E-associated kinase activity. Exponentially growing RIE-1 cells
stably expressing the indicated protein were harvested, cyclin
E-associated kinase activity was determined by immunoprecipitation
(IP) of cyclin E, and phosphorylation of histone H1 was
determined in an in vitro kinase assay. Recombinant Sf9
insect cell-expressed cyclin-E/CDK2 was assayed in parallel as an
internal control for the in vitro kinase assay. Ras utilizes
Raf-independent pathways to up-regulate cyclin E-associated kinase
activity. C, Ras, but not Raf, activation causes an increase
in CDK4 kinase activity. Exponentially growing RIE-1 cells stably
expressing the indicated protein were harvested, CDK4 was
immunoprecipitated, and phosphorylation of recombinant GST-Rb fusion
protein was determined in an in vitro assay. Data shown are
representative of at least three independent experiments.
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