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| Título: | Chaperone proteostasis in Parkinson's disease: stabilization of the Hsp70/α-synuclein complex by Hip |
Autor: | Roodveldt, Cintia CSIC ORCID; Fernández Montesinos, Rafael CSIC; Pozo, David CSIC ORCID; Dobson, Christopher M. | Palabras clave: | Amyloid Hip Hsp70 Parkinson's disease α-synuclein |
Fecha de publicación: | 2009 | Editor: | Nature Publishing Group European Molecular Biology Organization |
Citación: | EMBO Journal 28(23): 3758-3770 (2009) | Resumen: | The ATP-dependent protein chaperone heat-shock protein 70 (Hsp70) displays broad anti-aggregation functions and has a critical function in preventing protein misfolding pathologies. According to in vitro and in vivo models of Parkinson's disease (PD), loss of Hsp70 activity is associated with neurodegeneration and the formation of amyloid deposits of α-synuclein (αSyn), which constitute the intraneuronal inclusions in PD patients known as Lewy bodies. Here, we show that Hsp70 depletion can be a direct result of the presence of aggregation-prone polypeptides. We show a nucleotide-dependent interaction between Hsp70 and αSyn, which leads to the aggregation of Hsp70, in the presence of ADP along with αSyn. Such a co-aggregation phenomenon can be prevented in vitro by the co-chaperone Hip (ST13), and the hypothesis that it might do so also in vivo is supported by studies of a Caenorhabditis elegans model of αSyn aggregation. Our findings indicate that a decreased expression of Hip could facilitate depletion of Hsp70 by amyloidogenic polypeptides, impairing chaperone proteostasis and stimulating neurodegeneration. | Descripción: | 13 páginas, 6 figuras.-- et al. | Versión del editor: | http://dx.doi.org/10.1038/emboj.2009.298 | URI: | http://hdl.handle.net/10261/40966 | DOI: | 10.1038/emboj.2009.298 | ISSN: | 0261-4189 | E-ISSN: | 1460-2075 |
| Aparece en las colecciones: | (CABIMER) Artículos |
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