S-Nitrosylation of Parkin Regulates Ubiquitination and Compromises Parkin's Protective Function

+ See all authors and affiliations

Science  28 May 2004:
Vol. 304, Issue 5675, pp. 1328-1331
DOI: 10.1126/science.1093891

You are currently viewing the abstract.

View Full Text


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.

View Full Text

Related Content