Protein Networks

NON-COMMUNICABLE DISEASES / Cancer

Research Interests

High throughput proteomics, mass spectrometry, signal transduction, protein-protein interactions, tumorigenesis

Description of Research

The goal of the laboratory is to understand how protein complexes regulate cellular behavior. Inside the cell the majority of proteins can be found in highly interactive networks. The architecture of the cellular network and how it changes in response to the cellular environment is critical for the normal physiological functioning of the cell. In fact, these networks are responsible for the robustness and adaptability of living cells and perturbations to these networks result in pathological conditions such as cancer and neurological disorders. The response of the network to a stimulis is largely driven by the formation of new, transitory interactions, which are typically regulated by post translational modifications. Mass spectrometry is one of the most powerful techniques to uncover the architecture of these networks and how the network responds to perturbation. The laboratory uses high throughput mass spectrometry to gain insights into the protein interaction networks from a variety of normal and pathological conditions.

In particular, the studies in the laboratory have focused on the role of Ubiquitination in the response to DNA damage.  Importantly, DNA damage induces the formation of many new protein complexes and Ubiquitin functions as a scaffold, or bridge, to hold these complexes together.  As part of this work, the laboratory has uncovered a novel Ubiquitin binding domain, which functions only in DNA replication and repair. Furthermore, this Ubiquitin binding domain functions synergistically with other domains to direct the formation of Ubiquitin dependent complexes.

Recent Publications