S -Nitrosylation of Parkin Regulates Ubiquitination and Compromises Parkin's Protective Function-Reference-Cited by-同舟云学术

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

Published:2004-05-28 Issue:5675 Volume:304 Page:1328-1331
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Chung Kenny K. K.¹²³⁴⁵,Thomas Bobby¹²³⁴⁵,Li Xiaojie¹²³⁴⁵,Pletnikova Olga¹²³⁴⁵,Troncoso Juan C.¹²³⁴⁵,Marsh Laura¹²³⁴⁵,Dawson Valina L.¹²³⁴⁵,Dawson Ted M.¹²³⁴⁵

Affiliation:

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

2. Department of Neurology, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.

3. Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.

4. Department of Psychiatry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.

5. Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.

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.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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