Acetylation of MnSOD directs enzymatic activity responding to cellular nutrient status or oxidative stress

Ozkan Ozden, Seong Hoon Park, Hyun Seok Kim, Haiyan Jiang, Mitchell C. Coleman, Douglas R. Spitz, David Gius

Research output: Contribution to journalReview articlepeer-review

122 Scopus citations

Abstract

A fundamental observation in biology is that mitochondrial function, as measured by increased reactive oxygen species (ROS), changes significantly with age, suggesting a potential mechanistic link between the cellular processes governing longevity and mitochondrial metabolism homeostasis. In addition, it is well established that altered ROS levels are observed in multiple age-related illnesses including carcinogenesis, neurodegenerative, fatty liver, insulin resistance, and cardiac disease, to name just a few. Manganese superoxide dismutase (MnSOD) is the primary mitochondrial ROS scavenging enzyme that converts superoxide to hydrogen peroxide, which is subsequently converted to water by catalase and other peroxidases. It has recently been shown that MnSOD enzymatic activity is regulated by the reversible acetylation of specific, evolutionarily conserved lysine(s) in the protein. These results, suggest for the first time, that the mitochondria contain bidirectional posttranslational signaling networks, similar to that observed in the cytoplasm and nucleus, and that changes in lysine acetylation alter MnSOD enzymatic activity. In addition, these new results demonstrate that the mitochondrial anti-aging or fidelity/sensing protein, SIRT3, responds to changes in mitochondrial nutrient and/or redox status to alter the enzymatic activity of specific downstream targets, including MnSOD that adjusts and/or maintains ROS levels as well as metabolic homeostatic poise.

Original languageEnglish
Pages (from-to)102-107
Number of pages6
JournalAging
Volume3
Issue number2
DOIs
StatePublished - Feb 2011

Keywords

  • Acetylation
  • Mitochondria
  • MnSOD
  • Sirt3

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