Measuring Cellular Protein Dynamics During Stress Using Quantitative Proteomics
Cells are continuously exposed to various stresses originating from their own function, environmental changes, and pathogens. To understand the cellular responses to stresses, molecular systems approaches are required to assess and integrate the various global and molecular changes. Quantitative proteomics has proven particularly powerful to directly monitor underlying changes in protein abundance and modifications. Christian Münch, of Goethe University, and his team focus on applying quantitative proteomics to study stress responses, such as proteostasis perturbation and infection with pathogens. To be able to determine the highly dynamic and time-resolved effects of stresses, the team developed proteomics tools capable of quantifying these conditions for the translatome (mePROD) and mitochondrial protein import (mePRODmt). These approaches combine TMT-based multiplexing with pulse-SILAC labelling of the nascent proteome and booster signals to enhance signals of interest. Christian will show examples of how these approaches allow novel insight and therapeutic strategies for general cellular stress responses, infection and cancer.