Proteins known as oligomeric chaperones help suppress the formation of misshaped proteins that cause a variety of degenerative and neurodegenerative diseases, s
Credit: UT Southwestern Medical Center
DALLAS - Feb. 11, 2021 - A study led by UT Southwestern has identified a mechanism that controls the activity of proteins known as chaperones, which guide proteins to fold into the right shapes. The findings, published online today in
Nature Communications, could shed light on hundreds of degenerative and neurodegenerative diseases caused by protein misfolding, such as Alzheimer s, Parkinson s, and Huntington s, potentially leading to new treatments for these devastating conditions.
Every protein in the body is originally produced in a linear chain, with amino acid building blocks strung together one after another. But to fulfill their roles in cells, explains study leader Lukasz Joachimiak, Ph.D., assistant professor in the Center for Alzheimer s and Neurodegenerative Diseases at UT Southwestern, these chains need to fold into precise shapes. Chaperones help proteins accomplish this by protecting their vulnerable portions while they shift i