Calnexin Inhibitors

Calnexin is an integral membrane protein found predominantly in the endoplasmic reticulum (ER). Playing a crucial role in protein folding and quality control, calnexin binds to glycoproteins as they are translocated into the ER, ensuring that only properly folded proteins proceed through the secretory pathway. Its function is especially significant in the context of the calnexin/calreticulin cycle, a key process in monitoring and ensuring protein folding within the ER. This cycle is essential for cellular homeostasis, as the ER is a major site for the synthesis of membrane-bound and secreted proteins. Misfolded proteins can be harmful for the cell, leading to stress responses or even cell death, so the role of chaperones like calnexin in quality control is of paramount importance. Calnexin inhibitors are compounds that target and impede the function of calnexin. By inhibiting calnexin, these compounds can disrupt the protein folding process within the ER, leading to the accumulation of misfolded proteins. Given calnexin's pivotal role in protein homeostasis, its inhibitors can profoundly affect cellular functions, especially in cells with high secretory activity. These inhibitors offer a way to study the intricacies of protein folding, ER stress, and the cellular responses to such stress.