Grant: Travel Awards - Institute Community Support

The Myc family of proteins are known to be deregulated in a large variety of cancers. Mechanisms responsible for the deregulation of the activity of Myc family members in cancer are not well understood. A number of protein-protein interactions have been suggested to promote the oncogenic activity of Myc. Mapping the protein-protein interactions that support the aberrant activity of Myc family of oncoproteins in cancer is of high interest. A new analytical, mass spectrometry-based technique, BioID-MS, which relies on proximity-based biotin labeling, has recently emerged as a key advance for the characterization of protein-protein interactions in living cells. We are reporting a new application of the BioID-MS technique for the characterization of c-Myc interactors in human cell line in vivo. Using the in vivo BioID assay, we were able to identify more than 30 known c-Myc interactors. We were further able to identify more than 100 novel high-confidence c-Myc interactors. Using publically available datasets we were able to map some of the new high-confidence interactors to binding sites with c-Myc throughout the genome. We validated the Myc-CHD8 interaction using a number of biochemical approaches.These findings suggest that the BioID-MS technique can be used to map the Myc interactome and contribute to a greater understanding of Myc regulation by protein-protein interactions. We are further interested in exploring the possibility of targeting these interactors using small molecule therapeutic molecules for targeting cancers with deregulated Myc activity.