Copper chaperone blocks amyloid formation via ternary complex.
Q Rev Biophys
; 51: e6, 2018 01.
Article
en En
| MEDLINE
| ID: mdl-30912493
ABSTRACT
Protein misfolding in cells is avoided by a network of protein chaperones that detect misfolded or partially folded species. When proteins escape these control systems, misfolding may result in protein aggregation and amyloid formation. We here show that aggregation of the amyloidogenic protein α-synuclein (αS), the key player in Parkinson's disease, is controlled by the copper transport protein Atox1 in vitro. Copper ions are not freely available in the cellular environment, but when provided by Atox1, the resulting copper-dependent ternary complex blocks αS aggregation. Because the same inhibition was found for a truncated version of αS, lacking the C-terminal part, it appears that Atox1 interacts with the N-terminal copper site in αS. Metal-dependent chaperoning may be yet another manner in which cells control its proteome.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Cobre
/
Metalochaperonas
/
Amiloide
Límite:
Humans
Idioma:
En
Revista:
Q Rev Biophys
Año:
2018
Tipo del documento:
Article
País de afiliación:
Suecia