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S-nitrosylation regulates mitochondrial quality control via activation of parkin

Scientific Reports, ISSN: 2045-2322, Vol: 3, Issue: 1, Page: 2202
2013
  • 81
    Citations
  • 0
    Usage
  • 88
    Captures
  • 0
    Mentions
  • 21
    Social Media
Metric Options:   Counts1 Year3 Year

Metrics Details

  • Citations
    81
  • Captures
    88
  • Social Media
    21
    • Shares, Likes & Comments
      21
      • Facebook
        21

Article Description

Parkin, a ubiquitin E3 ligase of the ring between ring fingers family, has been implicated in mitochondrial quality control. A series of recent reports have suggested that the recruitment of parkin is regulated by phosphorylation. However, the molecular mechanism that activates parkin to induce mitochondrial degradation is not well understood. Here, and in contrast to previous reports that S-nitrosylation of parkin is exclusively inhibitory, we identify a previously unrecognized site of S-nitrosylation in parkin (Cys323) that induces mitochondrial degradation. We demonstrate that endogenous S-nitrosylation of parkin is in fact responsible for activation of its E3 ligase activity to induce aggregation and degradation. We further demonstrate that mitochondrial uncoupling agents result in denitrosylation of parkin, and that prevention of denitrosylation restores mitochondrial degradation. Our data indicates that NO both positive effects on mitochondrial quality control, and suggest that targeted S-nitrosylation could provide a novel therapeutic strategy against Parkinson's disease.

Bibliographic Details

Ozawa, Kentaro; Komatsubara, Akira T; Nishimura, Yuhei; Sawada, Tomoyo; Kawafune, Hiroto; Tsumoto, Hiroki; Tsuji, Yuichi; Zhao, Jing; Kyotani, Yoji; Tanaka, Toshio; Takahashi, Ryosuke; Yoshizumi, Masanori

Springer Science and Business Media LLC

Multidisciplinary

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