Mitochondrial Protein Acylation and Intermediary Metabolism: Regulation by Sirtuins and Implications for Metabolic Disease *
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 287, Issue: 51, Page: 42436-42443
2012
- 184Citations
- 199Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations184
- Citation Indexes184
- 184
- CrossRef160
- Captures199
- Readers199
- 199
Review Description
The sirtuins are a family of NAD + -dependent protein deacetylases that regulate cell survival, metabolism, and longevity. Three sirtuins, SIRT3–5, localize to mitochondria. Expression of SIRT3 is selectively activated during fasting and calorie restriction. SIRT3 regulates the acetylation level and enzymatic activity of key metabolic enzymes, such as acetyl-CoA synthetase, long-chain acyl-CoA dehydrogenase, and 3-hydroxy-3-methylglutaryl-CoA synthase 2, and enhances fat metabolism during fasting. SIRT5 exhibits demalonylase/desuccinylase activity, and lysine succinylation and malonylation are abundant mitochondrial protein modifications. No convincing enzymatic activity has been reported for SIRT4. Here, we review the emerging role of mitochondrial sirtuins as metabolic sensors that respond to changes in the energy status of the cell and modulate the activities of key metabolic enzymes via protein deacylation.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925820437366; http://dx.doi.org/10.1074/jbc.r112.404863; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84871107379&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/23086951; http://www.jbc.org/lookup/doi/10.1074/jbc.R112.404863; https://syndication.highwire.org/content/doi/10.1074/jbc.R112.404863; https://linkinghub.elsevier.com/retrieve/pii/S0021925820437366; https://dx.doi.org/10.1074/jbc.r112.404863; http://www.jbc.org/cgi/doi/10.1074/jbc.R112.404863; http://www.jbc.org/content/287/51/42436.abstract; http://www.jbc.org/content/287/51/42436.full; http://www.jbc.org/content/287/51/42436.full.pdf; http://www.jbc.org/content/287/51/42436; http://www.jbc.org/article/S0021925820437366/abstract; http://www.jbc.org/article/S0021925820437366/fulltext; http://www.jbc.org/article/S0021925820437366/pdf; https://www.jbc.org/article/S0021-9258(20)43736-6/abstract; https://www.jbc.org/content/287/51/42436
American Society for Biochemistry & Molecular Biology (ASBMB)
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