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• W2000290369 endingPage "8963" @default.
• W2000290369 startingPage "8960" @default.
• W2000290369 abstract "A variety of extracellular signals lead to the phosphorylation and activation of mitogen-activated protein kinases (MAP kinases). An activator of MAP kinases, Mek1, phosphorylates MAP kinases at threonine and tyrosine residues and is itself phosphorylated at serine-218 and -222 by the protooncogene product Raf-1. By introducing negatively charged residues that may mimic the effect of phosphorylation at positions 218 and 222, we have activated the capacity of Mek1 to phosphorylate MAP kinase by > 100-fold. The most effective activation by a single substitution resulted from the introduction of aspartate at position 218, whereas the introduction of either aspartate or glutamate at position 222 was ineffective. Expression of the activated Mek1 phosphorylation-site mutants in COS-7 cells led to the activation of MAP kinase in the cells and resulted in an increase in the mass of the transfected COS-7 cell population, suggesting an important role of Mek1 in the transduction of mitogenic signals." @default.
• W2000290369 created "2016-06-24" @default.
• W2000290369 creator A5027446790 @default.
• W2000290369 creator A5087888208 @default.
• W2000290369 date "1994-09-13" @default.
• W2000290369 modified "2023-10-17" @default.
• W2000290369 title "Constitutive activation of Mek1 by mutation of serine phosphorylation sites." @default.
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• W2000290369 doi "https://doi.org/10.1073/pnas.91.19.8960" @default.
• W2000290369 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/44726" @default.
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