BioCentury
ARTICLE | Targets & Mechanisms

Sorting out α-synuclein

Two studies link different forms of α-synuclein to PD initiation and progression

July 9, 2015 7:00 AM UTC

Studies by two independent groups propose a new hypothesis about how α-synuclein contributes to Parkinson's disease, suggesting that normal tetramers of the protein with α-helical structure break up into unfolded monomers, then regroup into toxic ribbon and fibril structures that spread from neuron to neuron to propagate the pathology throughout the brain. The findings point to tetramer stabilization as a possible therapeutic strategy, and emphasize the importance of determining which misfolded forms are most prevalent in patients.

Until now, α-synuclein has been linked to PD, but it hasn't been clear how mutations in the protein cause the disease or whether different misfolded forms of α-synuclein give rise to distinct pathologies. ...