Shanshan Liu and Mark Gad developed a liposome-based transport assay to characterize SLC33A1 transport activity in the endoplasmic reticulum.
Glutathione regulates protein folding in the ER
Rockefeller University researchers discovered that glutathione acts as a crucial proofreader ensuring proteins in the endoplasmic reticulum are folded correctly. The finding builds on prior work by Kivanç Birsoy’s lab identifying glutathione’s role in mitochondrial iron regulation and cancer metastasis.
Method enabled direct observation of ER chemistry
Liu developed a new method to rapidly profile the chemical landscape within the endoplasmic reticulum, allowing direct observation of organelle functions. The team used this approach after wondering about glutathione’s impact in the ER based on its known role in maintaining homeostasis with mitochondria.
ER requires oxidized glutathione balance
Unlike mitochondria where reduced glutathione dominates, the endoplasmic reticulum prefers an oxidized environment for protein folding. The researchers sought to calibrate the optimal glutathione ratio in this compartment.
What is SLC33A1?
SLC33A1 is a transporter that shuttles glutathione to where it’s needed in the cell, as previously discovered by Birsoy’s team.
Who co-supervised Mark Gad?
Mark Gad is a Ph.D. Student jointly supervised by Kivanç Birsoy and Richard Hite of Memorial Sloan Kettering Cancer Center.