A significant proportion of proteins utilize the secretory pathway that begins with nascent proteins entering the endoplasmic reticulum (ER). Protein folding and maturation occur in the ER. Properly folded proteins proceed through the Golgi and are secreted to their final destinations.  However, improperly folded proteins accumulate in the ER and induce the unfolded protein response (UPR). The unfolded protein response (UPR) is a quality control mechanism that adjusts the ER protein folding capacity according to need. 

The main goal of this research project is to (i) gain an improved understanding of the UPR with respect to protein interactions in vivo by monitoring the spatial localization of scFv, a model unfolded protein, throughout the secretory pathway and (ii) analyze the cellular variability associated with UPR activation. Confocal microscopy combined with green fluorescent protein (GFP) technology will be used to evaluate induction of the UPR due to scFv accumulation in the ER. We will quantify individual cell variability by simultaneously monitoring levels of the GFP reporter for the UPR and fluorescent variant of scFv.