Portal de Periódicos da CAPES

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

2004; American Association for the Advancement of Science; Volume: 304; Issue: 5675 Linguagem: Inglês

10.1126/science.1093891

1095-9203

Kenny K. K. Chung, Bobby Thomas, Xiaojie Li, Olga Pletniková, Juan C. Troncoso, Laura Marsh, Valina L. Dawson, Ted M. Dawson,

Histone Deacetylase Inhibitors Research

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.