Scientists have identified a yeast protein that can promote spontaneous prion formation - a breakthrough that could lead to therapies for Alzheimer's, Parkinson's and even Huntington's.
Lsb2 - the unstable, short-lived protein is strongly induced by cellular stresses such as heat. Its properties also illustrate how cells have developed ways to control and regulate prion formation.
The aggregated form of proteins connected with several other neurodegenerative diseases such as Alzheimer's, Parkinson's and Huntington's can, in some circumstances, act like prions.
So the Emory University School of Medicine's finding provides insight into how the ways that cells deal with stress might lead to poisonous protein aggregation in human diseases.
"A direct human homolog of Lsb2 doesn't exist, but there may be a protein that performs the same function," said senior author Keith Wilkinson, PhD, professor of biochemistry at Emory University School of Medicine.
"The mechanism may say more about other types of protein aggregates than about classical prions in humans, This mechanism of seeding and growth may be more important for aggregate formation in diseases such as Huntington's," he added.
The study was recently published in the journal Molecular Cell.