Project Description
Almost one-third of cellular proteins fold inside the endoplasmic reticulum (ER) to attain their biological active forms before reaching their intended targets. Various stressful conditions, both extracellular and intracellular, disturb the normal protein folding function of ER, leading to the accumulation of unfolded protein inside the ER lumen, a state known as “ER stress”. ER stress triggers the activation of the protein kinase Slt2; however, the precise molecular function of Slt2 kinase in ER function remains elusive. Slt2 is known to phosphorylate numerous substrates, including the transcription factor Rlm1. In this study, we will investigate how phosphorylations of Rlm1 contribute to ER protein homeostasis.
Tasks and Responsibilites
Read relevant literatures
Join the lab meetings
Help keep the lab clean
Perform molecular and microbiological experiments
Interpret results in consulting with me