Localized activation of RTK/MAPK pathways during Drosophila development.
Receptor tyrosine kinase (RTK) signaling is mediated by a signaling cascade culminating in activation of mitogen-activated protein kinase (MAPK) by double phosphorylation on threonine and tyrosine residues. The pattern of MAPK activation can now be directly visualized in situ during embryonic and adult development using an antiserum is specific for the double phosphorylated form of MAPK (db-P MAPK). The pattern of MAPK activation detected by this antiserum in developing embryos and larval imaginal discs conforms remarkably well to the inferred pattern of known RTK function. In addition, db-P MAPK staining directly reveals features of signaling such as the range of signal spreading and the kinetics of RTK activation, which would be difficult to measure by other methods. The ability to visualize the output of RTK signaling also permits detailed establishment of epistatic relationships between signaling components of RTK cascades.
Bier
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Department of Biology, University of California, San Diego, La Jolla 92093-0349, USA. bier@biomail.ucsd.edu
D000818:Animals; D017871:Calcium-Calmodulin-Dependent Protein Kinases / Q000378:metabolism*; D004330:Drosophila / Q000196:embryology*; D029721:Drosophila Proteins; D004625:Embryo, Nonmammalian / Q000502:physiology*; D066246:ErbB Receptors / Q000378:metabolism; D020794:Receptor Protein-Tyrosine Kinases / Q000378:metabolism*; D017468:Receptors, Fibroblast Growth Factor / Q000378:metabolism; D015398:Signal Transduction
D029721:Drosophila Proteins; D017468:Receptors, Fibroblast Growth Factor; D066246:ErbB Receptors; D020794:Receptor Protein-Tyrosine Kinases; C080148:tor protein, Drosophila; D017871:Calcium-Calmodulin-Dependent Protein Kinases