Talk Title: Dissecting Phosphotyrosine Signaling Networks by Quantitative Phosphoproteomics
Jesper Olsen studied analytical chemistry at the University of Southern Denmark in Odense, and obtained his PhD in biochemistry and molecular biology in the laboratory of Matthias Mann. During his PhD he was involved in developing high-resolution mass spectrometry-based proteomics. He spent 4 years as a post-doctoral fellow at the Max Planck Institute for Biochemistry in Munich, where he developed a quantitative phosphoproteomics technology that was applied to global time-resolved analyses of cell signaling pathways in human cells.
In 2009, Jesper was recruited back to Denmark to head a group at the newly established Novo Nordisk Foundation Center for Protein Research (CPR) at University of Copenhagen. In 2012, he was promoted to vice director of CPR and in 2014 full professor. Jesper has received a number of research awards including the Max Planck Institute for Biochemistry Junior Research Award and HUPO Young Investigator Award in Proteomic Sciences.
Authors: Tanveer S. Batth, Moreno Papetti, Anamarija Pfeiffer, Chiara Francavilla and Jesper V. Olsen*
* Presenting author
Novo Nordisk Foundation Center for Protein Research (CPR), Faculty of Health and Medical Sciences, University of Copenhagen, Denmark.
Quantitative phosphoproteomics is emerging a powerful technology for global analysis of cellular signaling networks. In particular tyrosine phosphorylation (pTyr) 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. Here we employed quantitative phosphoproteomics to delineate receptor tyrosine kinase (RTK) signaling dynamics activated by different ligands leading to differential cellular outcome. We quantified thousands of pTyr events as a function of ligand and stimulation time and revealed RTK-specific regulation of pTyr sites on key adaptor and signaling molecules, which fine-tune cell migration and proliferation. These results, based on a multidisciplinary approach, which combines quantitative phosphoproteomics and functional assays, identify ligand-dependent mechanisms for the control of RTK signaling and for the specification of long-term cellular outcomes.