AI Summary
The research conducted at the University of Massachusetts Amherst has identified a key protein complex in cellular quality control, specifically focusing on the endoplasmic reticulum. The study sheds new light on the importance of the enzyme UGGT and partner protein Sep15 in the process of identifying and handling misfolded proteins within cells. This discovery could have significant implications for understanding and potentially treating various diseases linked to protein misfolding.
Anyone who’s tried to neatly gather a fitted sheet can tell you: folding is hard. Get it wrong with your laundry and the result can be a crumpled, wrinkled mess of fabric, but when folding fails among the approximately 7,000 proteins with an origami-like complexity that regulate essential cellular functions, the result can lead to one of a multitude of serious diseases ranging from emphysema and cystic fibrosis to Alzheimer’s disease. Fortunately, our bodies have a quality-control system that identifies misfolded proteins and marks them either for additional folding work or destruction, but how, exactly, this quality-control process functions is not entirely known. Researchers at the University of Massachusetts Amherst have now made a major leap forward in our understanding of how this quality-control system works by discovering the “hot spot” where all the action takes place. The research was published recently in the Proceedings of the National Academy of Sciences.
DNA may be the master blueprint for life, but it is of proteins that we’re built. While many of them are structurally simple, there are approximately 7,000 proteins that must be made in a cell’s secretory pathway and will be either dispersed throughout the cell or secreted to the extracellular space in order to perform their essential functions.
The story begins in the endoplasmic reticulum-;the cellular protein factories responsible for correctly building thousands of different proteins-;and involves two main players: an enzyme known as UGGT and the partner protein Sep15. Senior authors Daniel Hebert, professor of biochemistry and