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Kumar, R and Jangir, DK and Verma, G and Shekhar, S and Hanpude, P and Kumar, S and Kumari, R and Singh, N and Bhavesh, NS and Jana, NR and Maiti, TK (2017) S-nitrosylation of UCHL1 induces its structural instability and promotes α-synuclein aggregation. Scientific Reports.

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Abstract

Ubiquitin C-terminal Hydrolase-1 (UCHL1) is a deubiquitinating enzyme, which plays a key role in Parkinson’s disease (PD). It is one of the most important proteins, which constitute Lewy body in PD patient. However, how this well folded highly soluble protein presents in this proteinaceous aggregate is still unclear. We report here that UCHL1 undergoes S-nitrosylation in vitro and rotenone induced PD mouse model. The preferential nitrosylation in the Cys 90, Cys 152 and Cys 220 has been observed which alters the catalytic activity and structural stability. We show here that nitrosylation induces structural instability and produces amorphous aggregate, which provides a nucleation to the native α-synuclein for faster aggregation. Our findings provide a new link between UCHL1-nitrosylation and PD pathology.

Item Type: Article
Subjects: Neurodegenerative Disorders
Neuro-Oncological Disorders
Neurocognitive Processes
Neuronal Development and Regeneration
Informatics and Imaging
Genetics and Molecular Biology
Depositing User: Dr. D.D. Lal
Date Deposited: 09 May 2018 11:39
Last Modified: 18 May 2018 10:26
URI: http://nbrc.sciencecentral.in/id/eprint/352

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