MassIVE MSV000079116

Partial Public PXD002109

SIRT5 Regulates Lysine Malonylation

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Description

Protein acylation links energetic substrate flux with cellular adaptive responses. SIRT5 is a NAD+-dependent lysine deacylase and removes both succinyl and malonyl group. Using affinity enrichment and label free quantitative proteomics, we characterized the SIRT5-regulated lysine malonylome in wild type (WT) and Sirt5-/- mice. 1137 malonyllysine sites were identified across 430 proteins, with 183 sites (from 120 proteins) significantly increased in the Sirt5-/- animals. Pathway analysis identified glycolysis as the top SIRT5-regulated pathway. Importantly, glycolytic flux was diminished in primary hepatocytes from Sirt5-/- compared to WT mice. Substitution of malonylated lysine residue 184 in glyceraldehyde 3-phosphate dehydrogenase with glutamic acid, a malonyllysine mimic, suppressed its enzymatic activity. Comparison of our previous reports on acylation reveals that malonylation targets a different set of proteins than acetylation and succinylation. These data demonstrate that SIRT5 is a global regulator of lysine malonylation and provide a mechanism for regulation of energetic flux through glycolysis. [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: Lysine Malonylation

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Principal Investigators:
(in alphabetical order) 		Bradford W. Gibson
Submitting User: mrardin
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