Mitochondrial dysfunction in protein conformational disorders

Journal of genetics

SHLOMI BRIELLE^1¹  DANIEL KAGANOVICH^2,1² 

[1] Department of Cell and Developmental Biology, Hebrew University of Jerusalem, Givat Ram, Jerusalem, Israel^1;Department of Experimental Neurodegeneration, University Medical Center Gottingen, Waldweg 33, Göttingen, Germany^2

关键词: mitochondria;    Parkinson’s disease;    α-synuclein;    ageing;    neurodegene;   

DOI  :  

学科分类：生物科学（综合）

来源: Indian Academy of Sciences

【 摘 要 】

Protein aggregation is a hallmark of many neurodegenerative diseases. In Parkinson’s disease protein misfolding of α-synuclein involves conformational changes in the protein structure that often results in self-association and aggregation leading to accumulation of α-synuclein in neuronal cells. The underlying mechanisms by which aggregations can lead to impaired cellular functions are often not understood. Meanwhile, there is growing evidence that links mitochondrial dysfunction to Parkinson’s disease. As both mitochondria and protein aggregation of α-synuclein have been shown to play a major role in Parkinson’s disease, it seems likely that a converging mechanism exists that links the two pathways.

【 授权许可】

CC BY