SIRT3 regulates mitochondrial protein acetylation and intermediary metabolism.

Published

Journal Article (Review)

The sirtuins are a family of nicotinamide adenine dinucleotide (NAD(+))-dependent protein deacetylases that regulate cell survival, metabolism, and longevity. Humans have seven sirtuins (SIRT1-SIRT7) with distinct subcellular locations and functions. SIRT3 is localized to the mitochondrial matrix and its expression is selectively activated during fasting and calorie restriction. Activated SIRT3 deacetylates several key metabolic enzymes-acetyl-coenzyme A synthetase, long-chain acyl-coenzyme A (acyl-CoA) dehydrogenase (LCAD), and 3-hydroxy-3-methylglutaryl CoA synthase 2-and enhances their enzymatic activity. Disruption of SIRT3 activity in mice, either by genetic ablation or during high-fat feeding, is associated with accelerated development of metabolic abnormalities similar to the metabolic syndrome in humans. SIRT3 is therefore emerging as a metabolic sensor that responds to change in the energy status of the cell and modulates the activity of key metabolic enzymes via protein deacetylation.

Full Text

Duke Authors

Cited Authors

  • Hirschey, MD; Shimazu, T; Huang, J-Y; Schwer, B; Verdin, E

Published Date

  • 2011

Published In

Volume / Issue

  • 76 /

Start / End Page

  • 267 - 277

PubMed ID

  • 22114326

Pubmed Central ID

  • 22114326

Electronic International Standard Serial Number (EISSN)

  • 1943-4456

Digital Object Identifier (DOI)

  • 10.1101/sqb.2011.76.010850

Language

  • eng

Conference Location

  • United States