ROBUST AND COMPREHENSIVE PROTEIN-PROTEIN INTERACTION ANALYSIS WITH THE EVOSEP ONE
Available on demand
In this webinar we will explore the possibilities of using the Evosep One technology to perform protein-protein interaction analysis.
During this webinar Leonard Foster (University of British Colombia, Vancouver) and Lisa Jones (University of Maryland, Baltimore) will provide their insight into the use of Evosep One in the study of complex protein environments. Using very different approaches, both scientists will discuss their view on unravelling complex protein interactions and the how this data can assist in cause and effect analyses of the mammalian, c-elegans or cell systems studied.
AN ATLAS OF PROTEIN-PROTEIN INTERACTIONS ACROSS MOUSE TISSUES
TALK BY LEONARD FOSTER, ASSISTANT PROF. AT UNIVERSITY OF BRITISH COLUMBIA
Cellular processes arise from the dynamic organization of proteins in networks of physical interactions. Mapping the complete network of biologically relevant protein-protein interactions, the interactome, has therefore been a central objective of high-throughput biology. However, the dynamics of protein interactions across physiological contexts remain poorly understood.
Here, we develop a quantitative proteomic approach combining protein correlation profiling with stable isotope labelling of mammals (PCP-SILAM) to map the interactomes of seven mouse tissues. The resulting maps provide the first proteome-scale survey of interactome dynamics across mammalian tissues, revealing over 125,000 unique interactions at a quality comparable to the highest-quality human screens. We identify systematic suppression of cross-talk between the evolutionarily ancient housekeeping interactome and younger, tissue-specific modules. Rewiring of protein interactions across tissues is widespread, and rewired proteins are tightly regulated by multiple cellular mechanisms and implicated in disease.
Our study opens up new avenues to uncover regulatory mechanisms that shape in vivo interactome responses to physiological and pathophysiological stimuli in mammalian systems.
IN-CELL PROTEIN FOOTPRINTING COUPLED WITH MASS SPECTROMETRY FOR STRUCTURAL BIOLOGY ACROSS THE PROTEOME
TALK BY LISA JONES, ASSOCIATE PROFESSOR AT UNIVERSITY OF MARYLAND, BALTIMORE (UMB)
In recent years, protein footprinting coupled with mass spectrometry has been used to identify protein-protein interaction sites and regions of conformational change through modification of solvent accessible sites in proteins.
The footprinting method, fast photochemical oxidation of proteins (FPOP), utilizes hydroxyl radicals for protein modification. To date, FPOP has been used in vitro on relatively pure protein systems. We have further extended the FPOP method for in vivo analysis of proteins both in cells and in C. elegans, an animal model for human disease. We have optimized experimental conditions so that the method can modify thousands of proteins for structural biology across the proteome.