THE EFFECTS OF MISFOLDED PROTEIN STRESS ON DIFFERENT CELL TYPES IN C. ELEGANS

Proper management of protein folding and localization during the life of a cell is essential for its survival, and many human diseases are associated with disruption of this management. The nascent polypeptide-associated complex (NAC) is a two-subunit complex essential to the proper folding and localization of proteins during translation, and loss of this complex has been associated with significant cell stress and cell death. Specifically, NAC depletion generates misfolded protein stress, engaging the unfolded protein response (UPR), a cell survival mechanism that mitigates the damage misfolded protein stress generates in the endoplasmic reticulum (ER). We are using the nematode C. elegans as a model organism for the study of the NAC, depleting it to observe cell stress and cell death phenotypes associated with the resulting misfolded protein stress and UPR induction. C. elegans development has been thoroughly investigated, and proteins expressed in specific cell lineages can be fluorescently tagged and followed throughout the life of the worm. In addition, cell stress proteins associated with UPR induction are available as fluorescently tagged proteins. Using microscopy techniques, we are investigating the co-localization of UPR-induced proteins with cell-specific markers in NAC-depleted worms to better understand the differential responses of specific cell types to misfolded protein stress.

Additional Abstract Information

Student(s): Shvan M. Kareem, Courtney A. Matson, Erin Wallace

Department: Biology

Faculty Advisor: Dr. Kimberly Slekar, Dr. Tim Bloss

Type: Poster

Year: 2014