Article
Synergistic activities of multiple phosphotyrosine residues mediate full signaling from the Drosophila Torso receptor tyrosine kinase.
Proceedings of the National Academy of Sciences of the United States of America - 19 Jan 1999
Gayko U, Cleghon V, Copeland T, Morrison D K, Perrimon N
Abstract excerpt
Here, we identify four tyrosine residues (Y644, Y698, Y767, and Y772) that become phosphorylated after activation of the Torso (Tor) receptor tyrosine kinase. Previously, we characterized phosphotyrosine sites (P-Y630 and P-Y918). Of the six P-Y sites identified, three (Y630, Y644, and Y698) are...
Topics
- Animals
- Animals, Genetically Modified
- Drosophila
- Drosophila Proteins
- Embryonic Development
- Insect Proteins
- Mutation
- Phosphopeptides
- Phosphorylation
- Phosphotyrosine
- Receptor Protein-Tyrosine Kinases
- Recombinant Proteins
- Signal Transduction
- Structure-Activity Relationship