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

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

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578 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)1328-1331
Number of pages4
JournalScience
Volume304
Issue number5675
DOIs
StatePublished - May 28 2004

ASJC Scopus subject areas

  • General

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    Chung, K. K. K., Thomas, B., Li, X., Pletnikova, O., Troncoso, J. C., Marsh, L., Dawson, V. L., & Dawson, T. M. (2004). S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function. Science, 304(5675), 1328-1331. https://doi.org/10.1126/science.1093891