期刊
SCIENTIFIC REPORTS
卷 7, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/srep44558
关键词
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资金
- Regional Centre for Biotechnology
- Department of Biotechnology, Government of India, ICGEB, New Delhi
- NII New Delhi
- University Grant Commission (UGC)
- Department of Biotechnology (DBT)
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 alpha-synuclein for faster aggregation. Our findings provide a new link between UCHL1-nitrosylation and PD pathology.
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