Affiliation: NYU Abu Dhabi
Education: BS, New York University Abu Dhabi
Research Areas: Unfolded Protein Response, Liver, Activating transcription factor 6, Toxicology, Development
Nouf Khan is a Research Assistant at the Sadler lab. She started at the Sadler lab as an undergraduate researcher in 2018. She studied the underlying mechanism of how oxidative stress triggers the unfolded protein response during arsenic exposure. While conducting her graduation thesis, she began her project in characterizing the function of ATF6 during development and stress. ATF6 is one of the three main pathways that regulate the unfolded protein response. However, it is the most understudied pathway. Nouf mainly investigates the impact of the loss of ATF6 and aims to continue this endeavor as Sadler's lab's new research assistant.
Cells can respond to stress in various ways ranging from protective to destructive processes to preserve the homeostatic nature of the cell. These responses involve changes in protein function, gene expression, energy utilization, induction of autophagy, and cell death activation. One of the main cellular stress responses is the unfolded protein response (UPR) which is a key process of Endoplasmic Reticulum stress, and it is triggered by the accumulation of dysfunctional protein folding. There are three main UPR pathways IRE1, PERK, AND ATF6. Atf6 is an Endoplasmic Reticulum localized protein often activated upon accumulation of misfiled proteins that result to proteolytic cleavage. Then, Atf6 is transported to the Golgi apparatus and cleaved by site specific proteases. This allows for the cytosolic portion, a bZIP transcription factor to migrate to the nucleus and activate a set of UPR target chaperones. So far, Atf6 function has mostly been characterized in the context of proteostasis however, the Sadler lab is focusing on investigating the other functions of Atf6 in the context of development and stress response.