Journal
FRONTIERS IN PHYSIOLOGY
Volume 5, Issue -, Pages -Publisher
FRONTIERS MEDIA SA
DOI: 10.3389/fphys.2014.00301
Keywords
acetylation; succinylation; malonylation; glutarylation; heart; sirtuin; Sirt3; Sirt5
Categories
Funding
- NIH [R21HL108052]
- American Heart Association National Scientist Development Grant [12SDG12060056]
- Zegar Family Foundation
- [HH5N268201000032C]
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Lysine modifications have been studied extensively in the nucleus, where they play pivotal roles in gene regulation and constitute one of the pillars of epigenetics. In the cytoplasm, they are critical to proteostasis. However, in the last decade we have also witnessed the emergence of mitochondria as a prime locus for post-translational modification (RIM) of lysine thanks, in large measure, to evolving proteomic techniques. Here, we review recent work on evolving set of RIM that arise from the direct reaction of lysine residues with energized metabolic thioester-coenzyme A intermediates, including acetylation, succinylation, malonylation, and glutarylation. We highlight the evolutionary conservation, kinetics, stoichiometry, and cross-talk between members of this emerging family of PTMs. We examine the impact on target protein function and regulation by mitochondrial sirtuins. Finally, we spotlight work in the heart and cardiac mitochondria, and consider the roles acetylation and other newly-found modifications may play in heart disease.
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