Maggie Kerwin

Research/Areas of Interest

ER proteostasis is critical in maintaining the delicate balance and regulation of protein folding, maturation and quality control within the ER. Disruptions in ER proteostasis, whether induced by cellular stress or mutations in ER proteins, can lead to the accumulation of misfolded or abnormal proteins within the ER, consequently triggering the unfolded protein response (UPR). UBXN1 is an adaptor protein for p97, an AAA-ATPase that functions in numerous ubiquitin-dependent protein quality control processes. Previous research conducted by our lab has established UBXN1 as a negative regulator of the UPR and its loss results in substantial enrichment of a subset of proteins involved in ER-quality control processes. Notably, UBXN1 has been shown to act as a translation repressor whose absence leads to increased translation under basal conditions, and this heightened translation persists in response to ER stress. My current research is focused on unraveling the mechanistic underpinnings of how UBXN1 exerts its control over translation in order to prevent ER stress and maintain proteostasis.