Anti-UGGT/UGT1 antibody

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

UGGT also known as UGT1 is a protein that catalyzes the addition of glucose to misfolded glycoproteins in the endoplasmic reticulum (ER). This enzyme weighs approximately 170 kDa and is found mainly in the ER. It functions by recognizing improperly folded proteins and facilitating their retention in the ER through tagging with a glucose moiety for quality control. The targeting of these proteins ensures only properly folded proteins proceed to the Golgi apparatus.

Biological function summary

UGGT/UGT1 plays an important role in the cellular quality control system. It works as part of the calnexin cycle interacting with chaperones like calnexin and calreticulin which recognize the glycosylated proteins. This cycle ensures that proteins fold correctly before they leave the ER. If proteins remain misfolded UGGT/UGT1 continues to add the glucose tag preventing their exit from the ER until correct folding occurs.

Pathways

UGGT/UGT1 is important for the proper functioning of the ER-associated degradation (ERAD) pathway and the unfolded protein response (UPR). In the ERAD pathway UGGT collaborates with proteins such as EDEM and mannosidase I recognizing and degrading misfolded glycoproteins. By doing so UGGT/UGT1 helps maintain cellular homeostasis balancing protein synthesis and degradation within the ER environment to prevent stress and potential damage.

Associated diseases and disorders

UGGT/UGT1 has connections to conditions like cystic fibrosis and certain congenital disorders of glycosylation. Cystic fibrosis involves improper protein folding where mutations lead to defective protein cycling and mismanagement of chloride channels like CFTR. In cases of congenital disorders of glycosylation UGGT/UGT1 interacts with proteins involved in glycosylation processes leading to altered glycoprotein profiles with varied clinical outcomes. Understanding UGGT/UGT1's interactions can aid in developing therapeutic strategies targeting protein misfolding.