Northwestern Medicine scientists have zeroed in on a cellular gatekeeper that may hold promise for treating abnormal protein accumulation in neurodegenerative diseases, according to a study published in Nature Communications. “In all neurodegenerative diseases, there is an accumulation of misfolded proteins,” said Robert Kalb, MD, the Joan and Paul Rubschlager Professor, chief of Neuromuscular Disease in the Ken and Ruth Davee Department of Neurology, and director of the Les Turner ALS Center, who was senior author of the study.

“We think that these misfolded proteins are a target for disease—the disease is actually driven by the accumulation of these misfolded proteins.”

In the current study, Kalb and his collaborators aimed to investigate the role of RAD23, a protein that is involved in the identification and disposal of damaged or misfolded proteins. Under normal circumstances, elimination of misfolded proteins is essential for maintaining a healthy collection of proteins in cells, a process known as protein homeostasis, or proteostasis.