There have been few studies of protein folding in the endoplasmic reticulum of intact mammalian cells. In the one case where the in vivo and in vitro folding pathways of a mammalian secretory protein have been compared, the folding of the human chorionic gonadotropin β subunit (hCG-β), the order of formation of the detected folding intermediates is the same. The rate and efficiency with which multidomain proteins such as hCG-β fold to native structure in intact cells is higher than in vitro, although intracellular rates of folding of the β subunit can be approached in vitro in the presence of an optimal redox potential and protein disulfide isomerase. Understanding how proteins fold in vivo may provide a new way to diagnose and treat human illnesses that occur due to folding defects.
- disease states related to protein misfolding
- hCG-β subunit as a model of secretory protein folding
- molecular chaperones
- protein misfolding
- role of disulfide bonds and N-linked glycosylation in protein folding, assembly, and secretion
ASJC Scopus subject areas
- Molecular Biology