Our group is interested in understanding mechanisms that maintain protein homeostasis within the cell. In particular we are interested in the role of the VCP AAA-ATPase in the recognition and degradation of ubiquitin-modified substrates. VCP is an abundant cellular chaperone that performs critical functions in diverse cellular programs such as ER associated degradation, autophagy, DNA damage responses and chromatin re-modeling. Importantly, VCP mutations are known to cause a spectrum of neurodegenerative disorders and its over-expression is prevalent in many cancers. Our recent proteomic profiling of VCP complexes demonstrates that VCP is targeted to diverse cellular structures and organelles via distinct adaptor proteins. We are interested in identifying new pathways that utilize VCP activity, determine its mechanism of action on substrates and identify new VCP targets. Our goal is to apply these findings to help understand its dysfunction in human disorders.