Scopus: 3 citas,
Copper(II) and the pathological H50Q α-synuclein mutant : environment meets genetics
Villar-Piqué, Anna (University Medical Centre Göottingen. Department of Neurodegeneration and Restorative Research)
Rossetti, Giulia (Jülich Forschungszentrum. Institut für Neurowissenschaften und Medizin)
Ventura i Zamora, Salvador (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Carloni, Paolo (Jülich Forschungszentrum. Institut für Neurowissenschaften und Medizin)
Fernández, Claudio O. (Max Planck Laboratory for Structural Biology, Chemistry and Molecular Biophysics of Rosario)
Outeiro, Tiago Fleming (University Medical Centre Göottingen. Department of Neurodegeneration and Restorative Research)
Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular

Fecha: 2017
Resumen: Copper is one of the metals described to bind the Parkinson disease-related protein α-synuclein (aSyn), and to promote its aggregation. Although histidine at position 50 in the aSyn sequence is one of the most studied copper-anchoring sites, its precise role in copper binding and aSyn aggregation is still unclear. Previous studies suggested that this residue does not significantly affect copper-mediated aSyn aggregation. However, our findings showed that the aggregation of the pathological H50Q aSyn mutant is enhanced by copper hints otherwise. Despite the inexistence of a model for aSyn H50Q-copper complexation, we discuss possible mechanisms by which this metal contributes to the misfolding and self-assembly of this particular aSyn mutant. Considering the genetic association of the H50Q mutation with familial forms of Parkinson disease, and the fact that copper homeostasis is deregulated in this disorder, understanding the interplay between both factors will shed light into the molecular and cellular mechanisms triggering the development and spreading of the aSyn pathology.
Derechos: Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, i la comunicació pública de l'obra, sempre que no sigui amb finalitats comercials, i sempre que es reconegui l'autoria de l'obra original. No es permet la creació d'obres derivades. Creative Commons
Lengua: Anglès
Documento: article ; recerca ; publishedVersion
Materia: α-synuclein ; Amyloid ; Copper ; H50Q mutation ; Parkinson disease ; Protein aggregation
Publicado en: Communicative & integrative Biology, Vol. 10, no. 1 (2017) , e127048, ISSN 1942-0889

PMID: 28289488
DOI: 10.1080/19420889.2016.1270484


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 Registro creado el 2018-02-08, última modificación el 2018-07-28



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