S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function - PubMed (original) (raw)

. 2004 May 28;304(5675):1328-31.

doi: 10.1126/science.1093891. Epub 2004 Apr 22.

Affiliations

• PMID: 15105460
• DOI: 10.1126/science.1093891

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

Kenny K K Chung et al. Science. 2004.

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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Comment in

• NO parkin in Parkinson's disease.
  Lancaster JR Jr. Lancaster JR Jr. Science. 2004 Jun 25;304(5679):1905; author reply 1905. doi: 10.1126/science.304.5679.1905a. Science. 2004. PMID: 15218128 No abstract available.
• Comment on "S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function".
  Lipton SA, Nakamura T, Yao D, Shi ZQ, Uehara T, Gu Z. Lipton SA, et al. Science. 2005 Jun 24;308(5730):1870; author reply 1870. doi: 10.1126/science.1110353. Science. 2005. PMID: 15976289 No abstract available.

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