[The information embedded into protein conformation: the mammalian prion protein is not the only one which "prionized"].
Basic research on prions and on protein and peptide aggregation generated a new vision of the pathologic mechanisms of many disorders regrouped under the term "proteinopathies". The latter include several neurodegenerative disorders (Alzheimer, Parkinson disease...) which could benefit for their diagnosis and therapeutics of this type of research. Importantly, the presence of proteins behaving like prions in yeast also contributed to the advance of knowledge in this area by showing that the transmission of a conformational information could be considered as a new epigenetic mechanism. In addition yeast models allow to study the molecular mechanism of protein aggregation, the role of accessory factors, like chaperones, and the screening of therapeutic agents.
Université Montpellier 2, Inserm, U710, 34095 Montpellier, France. karine.toupet@etud.univ-montp2.fr
Karine
K
Toupet
Sylvain
S
Lehmann
D000818:Animals; D008322:Mammals; D008958:Models, Molecular; D011328:Prions / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding
D011328:Prions