@article {843541,
	title = {A temperature-sensitive MEK mutation demonstrates the conservation of the signaling pathways activated by receptor tyrosine kinases.},
	journal = {Genes Dev},
	volume = {8},
	number = {18},
	year = {1994},
	month = {1994 Sep 15},
	pages = {2176-87},
	abstract = {
	MEK, a dual specificity threonine/tyrosine kinase, has been postulated to be a convergent point for signaling from receptor protein tyrosine kinases (RTKs) and G-protein-coupled receptors. In contrast to yeast and mammalian cells where several MEKs have been isolated, only one Drosophila MEK (D-Mek) has been characterized to date. Previous studies have shown that D-Mek acts in the Torso RTK signaling pathway. To demonstrate that D-Mek also operates downstream of other RTKs, we generated a temperature-sensitive allele of D-mek (D-mekts) by site-directed mutagenesis based on the amino acid change of a yeast cdc2ts mutation. Using D-mekts, we show that in addition to its role in Torso signaling, D-Mek operates in the Sevenless and in the Drosophila epidermal growth factor RTK pathways. Because loss-of-function mutations in D-mek and the upstream receptors give rise to similar phenotypes, it suggests that D-mek is the only MEK activated by Drosophila RTKs. In addition, we demonstrate that different RTK pathways respond differently to alteration in D-Mek activity.

},
	keywords = {Alleles, Amino Acid Sequence, Animals, Base Sequence, Conserved Sequence, DNA Primers, Drosophila, Female, Gene Expression Regulation, Developmental, Gene Expression Regulation, Enzymologic, Genes, Insect, Male, MAP Kinase Kinase 1, Mitogen-Activated Protein Kinase Kinases, Molecular Sequence Data, Mutagenesis, Site-Directed, Mutation, Protein-Serine-Threonine Kinases, Protein-Tyrosine Kinases, Receptor Protein-Tyrosine Kinases, Signal Transduction, Species Specificity, Temperature},
	issn = {0890-9369},
	author = {Hsu, J C and Perrimon, N}
}
