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    SIRT3 sirtuin 3 [ Homo sapiens (human) ]

    Gene ID: 23410, updated on 14-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Data show that Sirt1 and Sirt3 act on homologous substrates based on their evolutionary relationship.

    SIRT1 and SIRT3 deacetylate homologous substrates: AceCS1,2 and HMGCS1,2.
    Hirschey MD, Shimazu T, Capra JA, Pollard KS, Verdin E., Free PMC Article

    11/19/2011
    Mitochondrial deacetylase SIRT3 binds to, deacetylates and activates SOD2

    Tumour suppressor SIRT3 deacetylates and activates manganese superoxide dismutase to scavenge ROS.
    Chen Y, Zhang J, Lin Y, Lei Q, Guan KL, Zhao S, Xiong Y., Free PMC Article

    09/17/2011
    SirT3 acts to suppress the growth of tumors, at least in part through its ability to suppress ROS and HIF-1alpha.

    SirT3 suppresses hypoxia inducible factor 1α and tumor growth by inhibiting mitochondrial ROS production.
    Bell EL, Emerling BM, Ricoult SJ, Guarente L., Free PMC Article

    09/10/2011
    Human rSIRT3 was treated with 4-Hydroxynonenal, an endogenous product of lipid peroxidation to identify modified residues using nLC-MS/MS.

    4-Hydroxynonenal inhibits SIRT3 via thiol-specific modification.
    Fritz KS, Galligan JJ, Smathers RL, Roede JR, Shearn CT, Reigan P, Petersen DR., Free PMC Article

    09/10/2011
    SIRT3 substrates are involved in several metabolic pathways such as the urea cycle, ATP synthesis, and fatty acid oxidation.

    SIRT3 substrate specificity determined by peptide arrays and machine learning.
    Smith BC, Settles B, Hallows WC, Craven MW, Denu JM., Free PMC Article

    06/4/2011
    SIRT3 expression is reduced in human breast cancers, and its loss correlates with the upregulation of HIF1alpha target genes.

    SIRT3 opposes reprogramming of cancer cell metabolism through HIF1α destabilization.
    Finley LW, Carracedo A, Lee J, Souza A, Egia A, Zhang J, Teruya-Feldstein J, Moreira PI, Cardoso SM, Clish CB, Pandolfi PP, Haigis MC., Free PMC Article

    05/21/2011
    Observational study of gene-disease association and gene-gene interaction. (HuGE Navigator)

    MicroRNA-related genetic variations as predictors for risk of second primary tumor and/or recurrence in patients with early-stage head and neck cancer.
    Zhang X, Yang H, Lee JJ, Kim E, Lippman SM, Khuri FR, Spitz MR, Lotan R, Hong WK, Wu X., Free PMC Article

    12/5/2010
    Results indicate that Sirt3 functions as a downstream target gene of PGC-1alpha and mediates the PGC-1alpha effects on cellular ROS production and mitochondrial biogenesis.

    Sirtuin 3, a new target of PGC-1alpha, plays an important role in the suppression of ROS and mitochondrial biogenesis.
    Kong X, Wang R, Xue Y, Liu X, Zhang H, Chen Y, Fang F, Chang Y., Free PMC Article

    10/30/2010
    These studies identify a complex relationship between p53, SirT3, and chaperoning factor BAG-2 that may link the salvaging and quality assurance of the p53 protein for control of cellular fate independent of transcriptional activity.

    p53-induced growth arrest is regulated by the mitochondrial SirT3 deacetylase.
    Li S, Banck M, Mujtaba S, Zhou MM, Sugrue MM, Walsh MJ., Free PMC Article

    09/13/2010
    SIRT3 (sirtuin3) reduces lipid accumulation via AMP-Activated Protein Kinase activation in human hepatic cells

    SIRT3 reduces lipid accumulation via AMPK activation in human hepatic cells.
    Shi T, Fan GQ, Xiao SD.

    06/28/2010
    Report the impact of SIRT3 SNPs on protein stability and cellular energy metabolism.

    SIRT3 SNPs validation in 640 individuals, functional analyses and new insights into SIRT3 stability.
    Dransfeld CL, Alborzinia H, Wölfl S, Mahlknecht U.

    06/14/2010
    These results identify SIRT3 as a genomically expressed, mitochondria-localized tumor suppressor.

    SIRT3 is a mitochondria-localized tumor suppressor required for maintenance of mitochondrial integrity and metabolism during stress.
    Kim HS, Patel K, Muldoon-Jacobs K, Bisht KS, Aykin-Burns N, Pennington JD, van der Meer R, Nguyen P, Savage J, Owens KM, Vassilopoulos A, Ozden O, Park SH, Singh KK, Abdulkadir SA, Spitz DR, Deng CX, Gius D., Free PMC Article

    03/8/2010
    Results established that GATA2 and AP-1 Activator elements c-Jun/c-Fos act additively in modulating the SIRT3-VNTR enhancer function.

    Identification of GATA2 and AP-1 Activator elements within the enhancer VNTR occurring in intron 5 of the human SIRT3 gene.
    Bellizzi D, Covello G, Di Cianni F, Tong Q, De Benedictis G.

    02/15/2010
    the acetylated peptide is the first substrate to bind to SIRT3, before NAD(+).

    Crystal structures of human SIRT3 displaying substrate-induced conformational changes.
    Jin L, Wei W, Jiang Y, Peng H, Cai J, Mao C, Dai H, Choy W, Bemis JE, Jirousek MR, Milne JC, Westphal CH, Perni RB., Free PMC Article

    01/21/2010
    results show SIRT1 & SIRT3 are localized in different intracellular compartments, mainly nuclei & mitochondria; identified novel SIRT protein interacting partners which may be critically involved in anti-aging & metabolic regulatory activities of sirtuins

    Identification and characterization of proteins interacting with SIRT1 and SIRT3: implications in the anti-aging and metabolic effects of sirtuins.
    Law IK, Liu L, Xu A, Lam KS, Vanhoutte PM, Che CM, Leung PT, Wang Y.

    01/21/2010
    Observational study and meta-analysis of gene-disease association. (HuGE Navigator)

    Human longevity and 11p15.5: a study in 1321 centenarians.
    Lescai F, Blanché H, Nebel A, Beekman M, Sahbatou M, Flachsbart F, Slagboom E, Schreiber S, Sorbi S, Passarino G, Franceschi C., Free PMC Article

    04/29/2009
    Meta-analysis of gene-disease association. (HuGE Navigator)

    Genetic association analysis of 13 nuclear-encoded mitochondrial candidate genes with type II diabetes mellitus: the DAMAGE study.
    Reiling E, van Vliet-Ostaptchouk JV, van 't Riet E, van Haeften TW, Arp PA, Hansen T, Kremer D, Groenewoud MJ, van Hove EC, Romijn JA, Smit JW, Nijpels G, Heine RJ, Uitterlinden AG, Pedersen O, Slagboom PE, Maassen JA, Hofker MH, 't Hart LM, Dekker JM., Free PMC Article

    03/25/2009
    Data propose that SIRT3 and FOXO3a comprise a potential mitochondrial signaling cascade response pathway.

    SIRT3 interacts with the daf-16 homolog FOXO3a in the mitochondria, as well as increases FOXO3a dependent gene expression.
    Jacobs KM, Pennington JD, Bisht KS, Aykin-Burns N, Kim HS, Mishra M, Sun L, Nguyen P, Ahn BH, Leclerc J, Deng CX, Spitz DR, Gius D., Free PMC Article

    01/21/2010
    These studies underscore an essential role of SIRT3 in the survival of cardiomyocytes in stress situations.

    SIRT3 is a stress-responsive deacetylase in cardiomyocytes that protects cells from stress-mediated cell death by deacetylation of Ku70.
    Sundaresan NR, Samant SA, Pillai VB, Rajamohan SB, Gupta MP., Free PMC Article

    01/21/2010
    Results describe the substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5.

    Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5.
    Schlicker C, Gertz M, Papatheodorou P, Kachholz B, Becker CF, Steegborn C.

    01/21/2010
    full-length mouse SIRT3 protein is a 37 kDa mitochondrial precursor protein contrary to the previously suggested 29 kDa protein

    The human SIRT3 protein deacetylase is exclusively mitochondrial.
    Cooper HM, Spelbrink JN.

    01/21/2010
    Observational study of gene-disease association. (HuGE Navigator)See all PubMed (5) articles

    Genetic variants in nuclear-encoded mitochondrial genes influence AIDS progression.
    Hendrickson SL, Lautenberger JA, Chinn LW, Malasky M, Sezgin E, Kingsley LA, Goedert JJ, Kirk GD, Gomperts ED, Buchbinder SP, Troyer JL, O'Brien SJ.

    Investigation of genetic susceptibility factors for human longevity - a targeted nonsynonymous SNP study.
    Flachsbart F, Franke A, Kleindorp R, Caliebe A, Blanché H, Schreiber S, Nebel A.

    Genetic variation in healthy oldest-old.
    Halaschek-Wiener J, Amirabbasi-Beik M, Monfared N, Pieczyk M, Sailer C, Kollar A, Thomas R, Agalaridis G, Yamada S, Oliveira L, Collins JA, Meneilly G, Marra MA, Madden KM, Le ND, Connors JM, Brooks-Wilson AR.

    Coeliac disease-associated risk variants in TNFAIP3 and REL implicate altered NF-kappaB signalling.
    Trynka G, Zhernakova A, Romanos J, Franke L, Hunt KA, Turner G, Bruinenberg M, Heap GA, Platteel M, Ryan AW, de Kovel C, Holmes GK, Howdle PD, Walters JR, Sanders DS, Mulder CJ, Mearin ML, Verbeek WH, Trimble V, Stevens FM, Kelleher D, Barisani D, Bardella MT, McManus R, van Heel DA, Wijmenga C.

    A novel VNTR enhancer within the SIRT3 gene, a human homologue of SIR2, is associated with survival at oldest ages.
    Bellizzi D, Rose G, Cavalcante P, Covello G, Dato S, De Rango F, Greco V, Maggiolini M, Feraco E, Mari V, Franceschi C, Passarino G, De Benedictis G, Bellizzi D, Rose G, Cavalcante P, Covello G, Dato S, De Rango F, Greco V, Maggiolini M, Feraco E, Mari V, Franceschi C, Passarino G, De Benedictis G.

    03/13/2008
    Pro-apoptotic functioning of SIRT3 is selectively coupled with defined pathways regulating cell survival under basal conditions.

    SIRT3 is pro-apoptotic and participates in distinct basal apoptotic pathways.
    Allison SJ, Milner J.

    01/21/2010
    hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase. hSIRT3 is proteolytically processed in the mitochondrial matrix to a 28-kD product.

    The human silent information regulator (Sir)2 homologue hSIRT3 is a mitochondrial nicotinamide adenine dinucleotide-dependent deacetylase.
    Schwer B, North BJ, Frye RA, Ott M, Verdin E., Free PMC Article

    01/21/2010
    the underexpression of a human sirtuin gene seems to be detrimental for longevity as it occurs in model organisms.

    A novel VNTR enhancer within the SIRT3 gene, a human homologue of SIR2, is associated with survival at oldest ages.
    Bellizzi D, Rose G, Cavalcante P, Covello G, Dato S, De Rango F, Greco V, Maggiolini M, Feraco E, Mari V, Franceschi C, Passarino G, De Benedictis G, Bellizzi D, Rose G, Cavalcante P, Covello G, Dato S, De Rango F, Greco V, Maggiolini M, Feraco E, Mari V, Franceschi C, Passarino G, De Benedictis G.

    01/21/2010