Protein lipoylation: an evolutionarily conserved metabolic regulator of health and disease

Protein lipoylation: an evolutionarily conserved metabolic regulator of health and disease Available online at www.sciencedirect.com ScienceDirect Protein lipoylation: an evolutionarily conserved metabolic regulator of health and disease 1 1 Elizabeth A Rowland , Caroline K Snowden and Ileana M Cristea Lipoylation is a rare, but highly conserved lysine metabolic pathways. This theme of conservation is seen posttranslational modification. To date, it is known to occur on across the lipoylated complexes, the proteins that add or only four multimeric metabolic enzymes in mammals, yet these remove this modification, as well as the function of proteins are staples in the core metabolic landscape. The lipoylation [4 ,5,6,7 ,8 ]. Given this striking evolutionary dysregulation of these mitochondrial proteins is linked to a conservation for this rare modification, it is perhaps not range of human metabolic disorders. Perhaps most striking is surprising that these lipoylated enzymes are critically that lipoylation itself, the proteins that add or remove the linked to maintenance of health and development of modification, as well as the proteins it decorates are all disease. PDH dysregulation is known to contribute to evolutionarily conserved from bacteria to humans, highlighting numerous human metabolic disorders, cancer, viral infec- the importance of this essential cofactor. Here, we discuss the tion, and Alzheimer’s disease [9,10 http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Current Opinion in Chemical Biology Elsevier

Protein lipoylation: an evolutionarily conserved metabolic regulator of health and disease

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Publisher
Elsevier
Copyright
Copyright © 2017 Elsevier Ltd
ISSN
1367-5931
D.O.I.
10.1016/j.cbpa.2017.11.003
Publisher site
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Abstract

Available online at www.sciencedirect.com ScienceDirect Protein lipoylation: an evolutionarily conserved metabolic regulator of health and disease 1 1 Elizabeth A Rowland , Caroline K Snowden and Ileana M Cristea Lipoylation is a rare, but highly conserved lysine metabolic pathways. This theme of conservation is seen posttranslational modification. To date, it is known to occur on across the lipoylated complexes, the proteins that add or only four multimeric metabolic enzymes in mammals, yet these remove this modification, as well as the function of proteins are staples in the core metabolic landscape. The lipoylation [4 ,5,6,7 ,8 ]. Given this striking evolutionary dysregulation of these mitochondrial proteins is linked to a conservation for this rare modification, it is perhaps not range of human metabolic disorders. Perhaps most striking is surprising that these lipoylated enzymes are critically that lipoylation itself, the proteins that add or remove the linked to maintenance of health and development of modification, as well as the proteins it decorates are all disease. PDH dysregulation is known to contribute to evolutionarily conserved from bacteria to humans, highlighting numerous human metabolic disorders, cancer, viral infec- the importance of this essential cofactor. Here, we discuss the tion, and Alzheimer’s disease [9,10

Journal

Current Opinion in Chemical BiologyElsevier

Published: Feb 1, 2018

References

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