α-Synuclein and huntingtin exon 1 amyloid fibrils bind laterally to the cellular membrane.
Gif-sur-Yvette, France. In Sci Rep, Dec 2015
By characterizing the binding properties of aggregates made of α-synuclein or huntingtin exon 1 protein displaying similar composition and structure but different lengths to mammalian cells we demonstrate that in both cases aggregates bind laterally to the cellular membrane, with aggregates extremities displaying little or no role in membrane binding.
Targeting Hsp90/Hsp70-based protein quality control for treatment of adult onset neurodegenerative diseases.
In Annu Rev Pharmacol Toxicol, 2014
Critical target proteins that unfold and aggregate in these diseases, such as the polyglutamine androgen receptor in spinal and bulbar muscular atrophy, huntingtin in Huntington's disease, α-synuclein in Parkinson's disease, and tau in Alzheimer's disease, are client proteins of heat shock protein 90 (Hsp90), and their turnover is regulated by the protein quality control function of the Hsp90/Hsp70-based chaperone machinery.