Journal
CELL METABOLISM
Volume 27, Issue 3, Pages 497-512Publisher
CELL PRESS
DOI: 10.1016/j.cmet.2018.01.016
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Funding
- R24 grant from NIDDK [R24 DK085610]
- Larry L. Hillblom Foundation
- NIH [T32 AG000266]
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Post-translational modification of lysine residues via reversible acylation occurs on proteins from diverse pathways, functions, and organisms. While nuclear protein acylation reflects the competing activities of enzymatic acyltransferases and deacylases, mitochondrial acylation appears to be driven mostly via a non-enzymatic mechanism. Three protein deacylases, SIRT3, SIRT4, and SIRT5, reside in the mitochondria and remove these modifications from targeted proteins in an NAD(+)-dependent manner. Recent proteomic surveys of mitochondrial protein acylation have identified the sites of protein acetylation, succinylation, glutarylation, and malonylation and their regulation by SIRT3 and SIRT5. Here, we review recent advances in this rapidly moving field, their biological significance, and their implications for mitochondrial function, metabolic regulation, and disease pathogenesis.
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