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Comment
. 2017 Jul;42(7):499-501.
doi: 10.1016/j.tibs.2017.05.008. Epub 2017 Jun 3.

For Certain, SIRT4 Activities!

Affiliations
Comment

For Certain, SIRT4 Activities!

Surinder Kumar et al. Trends Biochem Sci. 2017 Jul.

Abstract

Despite the fact that SIRT4 regulates important biological processes, its primary enzymatic activity has remained ambiguous. A recent study by Anderson, Huynh et al. has uncovered deacylase activities of SIRT4 towards newly described lysine modifications derived from reactive acyl-CoAs generated in leucine catabolism.

Keywords: HMGylation; MGcylation; MGylation; SIRT4; Sirtuins.

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Figures

Figure 1
Figure 1
Novel Enzymatic Activities of SIRT4, and Reported Subcellular Localization and Catalytic Activities of All Mammalian Sirtuins. (A) SIRT4 catalyzes removal of newly discovered protein modifications, 3-hydroxy-3-methylglutaryl (HMG)-lysine, 3-methylglutaryl (MG)-lysine and 3-methylglutaconyl (MGc)-lysine. (B) Mammalian sirtuin localization and reported catalytic activities. Some graphics in this figure were obtained and modified from Servier Medical Art from Servier (http://www.servier.com/Powerpoint-image-bank).

Comment on

  • SIRT4 Is a Lysine Deacylase that Controls Leucine Metabolism and Insulin Secretion.
    Anderson KA, Huynh FK, Fisher-Wellman K, Stuart JD, Peterson BS, Douros JD, Wagner GR, Thompson JW, Madsen AS, Green MF, Sivley RM, Ilkayeva OR, Stevens RD, Backos DS, Capra JA, Olsen CA, Campbell JE, Muoio DM, Grimsrud PA, Hirschey MD. Anderson KA, et al. Cell Metab. 2017 Apr 4;25(4):838-855.e15. doi: 10.1016/j.cmet.2017.03.003. Cell Metab. 2017. PMID: 28380376 Free PMC article.

References

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    1. Anderson KA, et al. SIRT4 is a lysine deacylase that controls leucine metabolism and insulin secretion. Cell Metab. 2017;25:838–855. e815. - PMC - PubMed

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