Mapping of signaling networks in boundary formation by quantitative mass spectrometry and RNAi
Claus Jorgensen1
1Samuel Lunenfeld Research Institute, Mount Sinai Hospital. Toronto, ON, CA
Directionality in protein signaling networks can be obtained through modulation of protein-protein interactions, enzymatic activity and sub-cellular localization. Phosphorylation of linear recognition motifs by kinases and subsequent binding of modular domains is an essential way for cells to translate external cues to changes in cellular behavior. To identify signaling events essential for tissue boundary formation and maintenance we undertook a quantitative mass spectrometric analysis of tyrosine phosphorylation networks and overlaid this with a functional RNAi approach. Through these approaches we have identified a high confidence core network essential for tissue boundary control.
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