S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function |
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Authors: | Chung Kenny K K Thomas Bobby Li Xiaojie Pletnikova Olga Troncoso Juan C Marsh Laura Dawson Valina L Dawson Ted M |
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Affiliation: | Institute for Cell Engineering, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. |
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Abstract: | Parkin is an E3 ubiquitin ligase involved in the ubiquitination of proteins that are important in the survival of dopamine neurons in Parkinson's disease (PD). We show that parkin is S-nitrosylated in vitro, as well as in vivo in a mouse model of PD and in brains of patients with PD and diffuse Lewy body disease. Moreover, S-nitrosylation inhibits parkin's ubiquitin E3 ligase activity and its protective function. The inhibition of parkin's ubiquitin E3 ligase activity by S-nitrosylation could contribute to the degenerative process in these disorders by impairing the ubiquitination of parkin substrates. |
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