Project Description
Unfolded protein response (UPR) is a cellular strategy to increase the protein folding capacity of cells in response to stress within the endoplasmic reticulum (ER). In human cells, three major UPR sensors Ire1, PERK and ATF6 work in concert by simultaneously activating intracellular signaling pathways and modulating a series of physiological processes to enhance the protein folding capacity of cells. In yeast Saccharomyces cerevisiae, Ire1 is known to be the only UPR sensor, which mediates splicing of HAC1 mRNA in the cytoplasm and derepresses its translation. Hac1 is a transcription factor that increases the expression of protein folding enzymes and chaperones, thus enhancing the protein folding capacity of cells. Recently, we showed that mitogen activated protein kinase (MAPK) Slt2 plays a significant role in yeast UPR. We also provide evidence that human extracellular signal-regulated kinase 1 (ERK1) served as a functional substitute for yeast Slt2 in the context of UPR. The student will explore the function of ERK1 in UPR.
Tasks and Responsibilites
Research activities:
1. Searching literatures for the ERK1 in both yeast and human cells
2. Analyzing the sequence and structures of ERK1 and ERK2
3. Attending the Dey Lab meeting as and when required
4. Conducting molecular and biochemical studies in the Dey Lab.
Desired Qualifications
None Listed.