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Ironing out misfolded proteins

Once produced by a living cell’s micromachinery, proteins need to be folded into certain shapes to function properly and prevent diseases like cystic fibrosis, cancer and neurodegenerative disorders. New research has yielded promising insights that could help prevent protein misfolding.
Ironing out misfolded proteins
Cells have a system called endoplasmic reticulum–associated degradation (ERAD), which destroys misfolded or unassembled proteins that could cause disease. Understanding how exactly the ERAD system works will be a major factor in treating diseases caused by incorrectly folded proteins.

The project 'Expanding the knowledge on mammalian endoplasmic reticulum-associated degradation' (MAMMALIAN ERAD) was funded by the EU to study how ERAD goes about destroying certain misfolded proteins with common mutations.

The project's research revealed that one enzyme in the ERAD system, gp78, is key in the degradation of the mutated protein associated with cystic fibrosis. This enzyme is thus an attractive target for potential therapies.

Researchers also looked at the interaction between gp78 and another enzyme, Hrd1. They found that Hrd1 is responsible for activating gp78 and other key ERAD machinery.

Furthermore, the study investigated misfolded proteinsinvolved in cystic fibrosis, Paget's disease of the bone and frontotemporal dementia. It is hoped that the insights gained here will help inform future research into potential therapies against these diseases.

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