Our lab studies the role of the valosin-containing protein (VCP), a AAA ATPase that is critical for various aspects of ubiquitin-dependent protein quality control. VCP interacts with a number of dedicated cellular proteins known as adaptors which differentially mediate its function. An important function of VCP is to facilitate degradation of misfolded proteins by the 26S proteasome. One important function of VCP is to prevent the accumulation of misfolded proteins in the lumen of the endoplasmic reticulum (ER). Accumulation of these misfiled species in the ER facilitates the activation of an ER specific stress response called the unfolded protein response (UPR). The UPR aims to alleviate the stress of protein accumulation through activation of various signaling pathways. I am currently investigating the role of VCP adaptor complexes in ER stress and the UPR.