From Simple English Wikipedia, the free encyclopedia

Sirtuin or Sir2 proteins are a class of enzymes that are important in cell biology.[1][2][3][4][5]

Sirtuins regulate important biological pathways in bacteria, archaea and eukaryotes. The name Sir2 comes from the yeast gene 'silent mating-type information regulation 2',[6] the gene responsible for cellular regulation in yeast.

Sirtuins influence many cellular processes like ageing, transcription, apoptosis, inflammation and stress resistance,[7] as well as energy efficiency and alertness during low-calorie situations.[8] Sirtuins can also control circadian clocks and mitochondrial biogenesis.

References[change | change source]

  1. North, Brian J.; Verdin, Eric (2004). "Sirtuins: Sir2-related NAD-dependent protein deacetylases". Genome Biology. 5 (5): 224. doi:10.1186/gb-2004-5-5-224. PMC 416462. PMID 15128440.
  2. Yamamoto, Hiroyasu; Schoonjans, Kristina; Auwerx, Johan (2007). "Sirtuin functions in health and disease". Mol. Endocrinol. 21 (8): 1745–55. doi:10.1210/me.2007-0079. PMID 17456799. S2CID 33994296.
  3. Du, Jintang; Zhou, Yeyun; Su, Xiaoyang; Yu, Jiu Jiu; Khan, Saba; Jiang, Hong; Kim, Jungwoo; Woo, Jimin; Kim, Jun Huyn; Choi, Brian Hyun; He, Bin; Chen, Wei; Zhang, Sheng; Cerione, Richard A.; Auwerx, Johan; Hao, Quan; Lin, Hening (2011). "Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase". Science. 334 (6057): 806–809. Bibcode:2011Sci...334..806D. doi:10.1126/science.1207861. PMC 3217313. PMID 22076378.
  4. Jiang, Hong; Khan, Saba; Wang, Yi; Charron, Guillaume; He, Bin; Sebastian, Carlos; Du, Jintang; Kim, Ray; Ge, Eva; Mostoslavsky, Raul; Hang, Howard C.; Hao, Quan; Lin, Hening (2013). "SIRT6 regulates TNF-α secretion through hydrolysis of long-chain fatty acyl lysine". Nature. 496 (7443): 110–113. Bibcode:2013Natur.496..110J. doi:10.1038/nature12038. PMC 3635073. PMID 23552949.
  5. Rack J.G.M. et al 2015 (2015). "Identification of a class of protein ADP-ribosylating sirtuins in microbial pathogens". Molecular Cell. 59 (2): 309–320. doi:10.1016/j.molcel.2015.06.013. ISSN 1097-4164. PMC 4518038. PMID 26166706.{{cite journal}}: CS1 maint: numeric names: authors list (link)
  6. EntrezGene 23410 [1]
  7. Preyat, Nicolas; Leo, Oberdan (2013). "Sirtuin deacylases: a molecular link between metabolism and immunity". J. Leuk. Biol. 93 (5): 669–680. doi:10.1189/jlb.1112557. PMID 23325925. S2CID 3070941.
  8. Satoh, A.; Brace, C. S.; Ben-Josef, G.; West, T.; Wozniak, D. F.; Holtzman, D. M.; Herzog, E. D.; Imai, S.-i. (2010). "SIRT1 promotes the central adaptive response to diet restriction through activation of the dorsomedial and lateral nuclei of the hypothalamus". Journal of Neuroscience. 30 (30): 10220–32. doi:10.1523/JNEUROSCI.1385-10.2010. PMC 2922851. PMID 20668205.