(116av) Evaluating the Unfolded Protein Response of Saccharomyces Cerevisiae

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.