Display Settings:

Format

Send to:

Choose Destination

    Science. 2004 May 28;304(5675):1328-31. Epub 2004 Apr 22.

    S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function.

    Chung KK, Thomas B, Li X, Pletnikova O, Troncoso JC, Marsh L, Dawson VL, Dawson TM.

    Institute for Cell Engineering, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.

    Comment in:

    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.

    PMID: 15105460 [PubMed - indexed for MEDLINE]

    Supplemental Content

    Click here to read