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Sirtuin 6

This gene encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity. The protein encoded by this gene is included in class IV of the sirtuin family. Alternative splicing results in multiple transcript variants.[provided by RefSeq, Jul 2010] (from NCBI)
Top mentioned proteins: Sir2, Histone, SIRT3, V1a, AGE
Papers on SIRT6
SIRT6 protects cardiomyocytes against ischemia/reperfusion injury by augmenting FoxO3α-dependent antioxidant defense mechanisms.
Jiang et al., Chengdu, China. In Basic Res Cardiol, Mar 2016
SIRT6, a member of the NAD(+)-dependent class III deacetylase sirtuin family, has been revealed to play important roles in promoting cellular resistance against oxidative stress.
SIRT6 deacetylates PKM2 to suppress its nuclear localization and oncogenic functions.
Das et al., New Delhi, India. In Proc Natl Acad Sci U S A, Feb 2016
UNASSIGNED: SIRT6 (sirtuin 6) is a member of sirtuin family of deacetylases involved in diverse processes including genome stability, metabolic homeostasis, and tumorigenesis.
SIRT6, oxidative stress, and aging.
Kennedy et al., Novato, United States. In Cell Res, Feb 2016
A new study published in Cell Research reports a novel role for the aging-associated SIRT6 deacetylase in the control of oxidative homeostasis in human mesenchymal stem cells.
SIRT6 safeguards human mesenchymal stem cells from oxidative stress by coactivating NRF2.
Liu et al., Beijing, China. In Cell Res, Feb 2016
UNASSIGNED: SIRT6 belongs to the mammalian homologs of Sir2 histone NAD(+)-dependent deacylase family.
The complex role of SIRT6 in carcinogenesis.
Cohen et al., Ramat Gan, Israel. In Carcinogenesis, Jan 2016
UNASSIGNED: SIRT6, a member of the mammalian sirtuins family, functions as a mono-ADP-ribosyl transferase and NAD(+)-dependent deacylase of both acetyl groups and long-chain fatty acyl groups.
Targeting aberrant cancer metabolism - The role of sirtuins.
Baer-Dubowska et al., Poznań, Poland. In Pharmacol Rep, Dec 2015
It was recently demonstrated that SIRT6 is a tumor suppressor that modulates aerobic glycolysis by repressing HIF1 transcription.
Sirtuin-dependent clock control: new advances in metabolism, aging and cancer.
Masri, Irvine, United States. In Curr Opin Clin Nutr Metab Care, Nov 2015
In addition to sirtuin (SIRT)1 and SIRT3, SIRT6 has been demonstrated as a critical regulator of circadian transcription that also serves as an interface with metabolic homeostasis.
The role of sirtuins in cardiac disease.
Sadoshima et al., Newark, United States. In Am J Physiol Heart Circ Physiol, Nov 2015
Sirt6 has also recently been demonstrated to attenuate cardiac hypertrophy, and Sirt7 is known to regulate apoptosis and stress responses in the heart.
Coupling circadian rhythms of metabolism and chromatin remodelling.
Sassone-Corsi et al., Irvine, United States. In Diabetes Obes Metab, Sep 2015
Specifically, the nicotinamide adenine dinucleotide (NAD)(+) -dependent deacetylases SIRT1 and SIRT6 have been linked to circadian control of gene expression.
The histone deacetylase SIRT6 controls embryonic stem cell fate via TET-mediated production of 5-hydroxymethylcytosine.
Mostoslavsky et al., Boston, United States. In Nat Cell Biol, May 2015
Here we demonstrate the interplay between the histone deacetylase sirtuin 6 (SIRT6) and the ten-eleven translocation enzymes (TETs).
Decreased expression of SIRT6 promotes tumor cell growth correlates closely with poor prognosis of ovarian cancer.
Li et al., In Eur J Gynaecol Oncol, 2014
SIRT6 is downregulated in tumor and acts as tumor suppressor.
Partitioning circadian transcription by SIRT6 leads to segregated control of cellular metabolism.
Sassone-Corsi et al., Irvine, United States. In Cell, 2014
Whereas SIRT1 exhibits diversity in deacetylation targets and subcellular localization, SIRT6 is the only constitutively chromatin-associated sirtuin and is prominently present at transcriptionally active genomic loci.
SIRT6 regulates TNF-α secretion through hydrolysis of long-chain fatty acyl lysine.
Lin et al., Ithaca, United States. In Nature, 2013
Here we show that human SIRT6 efficiently removes long-chain fatty acyl groups, such as myristoyl, from lysine residues.
SIRT6 puts cancer metabolism in the driver's seat.
Cantley et al., Boston, United States. In Cell, 2013
show that loss of the tumor suppressor SIRT6 transforms cells by activating tumor metabolism.
The histone deacetylase SIRT6 is a tumor suppressor that controls cancer metabolism.
Mostoslavsky et al., Boston, United States. In Cell, 2013
Here, we identify SIRT6 as a tumor suppressor that regulates aerobic glycolysis in cancer cells.
NAD+-dependent sirtuin 1 and 6 proteins coordinate a switch from glucose to fatty acid oxidation during the acute inflammatory response.
McCall et al., Winston-Salem, United States. In J Biol Chem, 2012
in TLR4-stimulated promonocytes SirT1 and SirT 6 support a switch from increased glycolysis to increased fatty acid oxidation as early inflammation converts to late inflammation.
Sirtuin 6 (SIRT6) rescues the decline of homologous recombination repair during replicative senescence.
Seluanov et al., Rochester, United States. In Proc Natl Acad Sci U S A, 2012
Sirtuin 6 (SIRT6) rescues the decline of homologous recombination repair during replicative senescence.
Nmnat2 protects cardiomyocytes from hypertrophy via activation of SIRT6.
Liu et al., Guangzhou, China. In Febs Lett, 2012
Data show that overexpression of Nmnat2 but not its catalytically inactive mutant blocked angiotensin II (Ang II)-induced cardiac hypertrophy, which was dependent on activation of SIRT6 through maintaining the intracellular NAD level.
The sirtuin SIRT6 regulates lifespan in male mice.
Cohen et al., Ramat Gan, Israel. In Nature, 2012
This study shows the regulation of mammalian lifespan by a sirtuin family member and has important therapeutic implications for age-related diseases
Association of the sirtuin and mitochondrial uncoupling protein genes with carotid plaque.
Rundek et al., Miami, United States. In Plos One, 2010
observed significant associations between genetic variants in the SIRT6 and UCP5 genes and atherosclerotic plaque
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