CanCell seminar with Jesper Olsen: "Defining Critical Switches in Oncogenic EGFR signaling by Quantitative Interaction Proteomics and Phosphoproteomics"

"Mass spectrometry (MS)-based proteomics including quantitative interaction proteomics and phosphoproteomics has revolutionized cell signaling in the past decade. We apply this technology to systems-wide analyses of tyrosine phosphorylation (pTyr), which is of great importance in eukaryotic cells due to its crucial role in regulating intracellular signaling networks controlling cell fate decisions such as proliferation, migration, differentiation, cell cycle progression and apoptosis. The receptor tyrosine kinase, EGFR, is often dysregulated in cancer, which makes phosphoproteins involved in the EGFR pathway attractive therapeutic targets. Based on a multidisciplinary approach, which combines in-vivo quantitative phosphoproteomics, interaction proteomics and functional assays, we identified critical cellular switches that control EGF-dependent mechanisms in wildtype and mutated EGF receptor signaling, which specify long-term cellular outcomes and the oncogenic properties of the receptor"