Differential signaling through p190 and p210 BCR-ABL fusion proteins revealed by interactome and phosphoproteome analysis

Using quantitative mass spectrometry approaches, we have interrogated the differences in p190BCR-ABL and p210BCR-ABL signaling. By integrating protein interaction data generated by the in vivo labeling technique of BioID with tyrosine phosphorylation profiling, we identified a set of molecules that are differentially regulated between to the two forms of BCR-ABL.