Genomes and Genes
Gene Symbol: SIRT2
Description: sirtuin 2
Alias: SIR2, SIR2L, SIR2L2, NAD-dependent deacetylase sirtuin-2, NAD-dependent protein deacetylase sirtuin-2, SIR2-like protein 2, regulatory protein SIR2 homolog 2, silent information regulator 2, sir2-related protein type 2, sirtuin type 2, sirtuin-2
Publications156 found, 100 shown here
- Modulation of sirtuins: new targets for antiageingMerce Pallas
Unitat de Farmacologia i Farmacognòsia i Institut de Biomedicina IBUB, Facultat de Farmacia, Universitat de Barcelona, Nucli Universitari de Pedralbes, E 08028 Barcelona, Spain
Recent Pat CNS Drug Discov 3:61-9. 2008..The protein implicated in this protective process is the silent information regulator 2 (SIR2, SIRT1 in mammals), an enzyme that belongs to a nicotinamide adenine dinucleotide (NAD)+-..
- The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylaseBrian J North
Department of Physiology, University of California, San Francisco, 94141, San Francisco, CA, USA
Mol Cell 11:437-44. 2003The silent information regulator 2 protein (Sir2p) of Saccharomyces cerevisiae is an NAD-dependent histone deacetylase that plays a critical role in transcriptional silencing...
- Proteomics-based identification of differentially expressed genes in human gliomas: down-regulation of SIRT2 geneMasaharu Hiratsuka
Department of Molecular and Cell Genetics, Graduate School of Medical Science, Tottori University, Nishimachi 86, Yonago, Tottori 683 8503, Japan
Biochem Biophys Res Commun 309:558-66. 2003..We then focused on the cytoskeleton-related protein, SIRT2 (sirtuin homologue 2) tubulin deacetylase, which was down-regulated in gliomas. SIRT2 is located at 19q13...
- SIRT2 maintains genome integrity and suppresses tumorigenesis through regulating APC/C activityHyun Seok Kim
Genetics of Development and Disease Branch, 10 9N105, National Institute of Diabetes, Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA
Cancer Cell 20:487-99. 2011..To investigate the physiological functions of SIRT2 in development and tumorigenesis, we disrupted Sirt2 in mice...
- Human histone deacetylase SIRT2 interacts with the homeobox transcription factor HOXA10Nancy S Bae
Laboratory of Molecular and Growth Regulation, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA
J Biochem 135:695-700. 2004..Currently, there is no report on the interacting protein partner of a human Sir2 homolog, SIRT2. Here we show for the first time that SIRT2 interacts with the homeobox transcription factor, HOXA10, which was ..
- Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activityR A Frye
Department of Pathology, University of Pittsburgh, Pittsburgh, Pennsylvania, 15240, USA
Biochem Biophys Res Commun 260:273-9. 1999..Recombinant E. coli cobB and human SIRT2 sirtuin proteins were able to cause radioactivity to be transferred from [32P]NAD to bovine serum albumin (BSA)...
- Multiple histone deacetylases and the CREB-binding protein regulate pre-mRNA 3'-end processingTadahiro Shimazu
Chemical Genetics Laboratory, Discovery Research Institute, RIKEN, Wako, Saitama 351 0198, Japan
J Biol Chem 282:4470-8. 2007..Whereas CBP acetylated these proteins, HDAC1, HDAC3, HDAC10, SIRT1, and SIRT2 were involved in in vivo deacetylation...
- Characterization of a human gene with sequence homology to Saccharomyces cerevisiae SIR2G Afshar
University of California, San Francisco, Radiation Oncology Research Laboratories, San Francisco, CA 94103, USA
Gene 234:161-8. 1999..In the present study, the complete sequence of a human gene, SIR2L, with homology to the yeast SIR2 gene is presented...
- Conserved metabolic regulatory functions of sirtuinsBjoern Schwer
Gladstone Institute of Virology and Immunology, San Francisco, CA 94158, USA
Cell Metab 7:104-12. 2008b>Silent information regulator 2 (Sir2) proteins, or sirtuins, are protein deacetylases/mono-ADP-ribosyltransferases found in organisms ranging from bacteria to humans...
- Interphase nucleo-cytoplasmic shuttling and localization of SIRT2 during mitosisBrian J North
Gladstone Institute of Virology and Immunology, University of California at San Francisco, California, United States of America
PLoS ONE 2:e784. 2007The human NAD+-dependent protein deacetylase SIRT2 resides predominantly in the cytoplasm where it functions as a tubulin deacetylase...
- Sirt2 interacts with 14-3-3 beta/gamma and down-regulates the activity of p53Yun Hye Jin
College of Pharmacy and Research Institute of Drug Development, Chonnam National University, Gwangju, Republic of Korea
Biochem Biophys Res Commun 368:690-5. 2008b>Sirt2 is a mammalian member of the Sirtuin family of NAD(+) (nicotinamide adenine dinucleotide)-dependent protein deacetylases. Although Sir-2...
- Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycleSylvia C Dryden
Program in Molecular Biology and Genetics, Karmanos Cancer Institute and Wayne State University, Detroit, Michigan 48201, USA
Mol Cell Biol 23:3173-85. 2003..Our functional studies of human SIRT2, a homolog of the product of the yeast SIR2 gene, indicate that it plays a role in mitosis...
- FISH-mapping and genomic organization of the NAD-dependent histone deacetylase gene, Sirtuin 2 (Sirt2)Susanne Voelter-Mahlknecht
Department of Hematology Oncology, University of Heidelberg Medical Center, D 69120 Heidelberg, Germany
Int J Oncol 27:1187-96. 2005..2 (SIRT2) is a nicotinamide adenine dinucleotide (NAD(+))-dependent deacetylase, which belongs to the Silent information regulator 2 (Sir2) family of sirtuin histone deacetylases (HDACs)...
- Conserved enzymatic production and biological effect of O-acetyl-ADP-ribose by silent information regulator 2-like NAD+-dependent deacetylasesMargie T Borra
Department of Biochemistry and Molecular Biology, Oregon Health and Sciences University, Portland, OR 97201 3098, USA
J Biol Chem 277:12632-41. 2002b>Silent information regulator 2 (Sir2) family of enzymes has been implicated in many cellular processes that include histone deacetylation, gene silencing, chromosomal stability, and aging...
- SIRT2, a tubulin deacetylase, acts to block the entry to chromosome condensation in response to mitotic stressT Inoue
Department of Human Genome Science, Graduate School of Medical Science, Tottori University, Yonago, Tottori, Japan
Oncogene 26:945-57. 2007We previously identified SIRT2, an nicotinamide adenine dinucleotide (NAD)-dependent tubulin deacetylase, as a protein downregulated in gliomas and glioma cell lines, which are characterized by aneuploidy...
- SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosisAlejandro Vaquero
Howard Hughes Medical Institute, Piscataway, NJ 08854, USA
Genes Dev 20:1256-61. 2006The mammalian cytoplasmic protein SirT2 is a member of the Sir2 family of NAD+-dependent protein deacetylases involved in caloric restriction-dependent life span extension...
- Substrate specificity and kinetic mechanism of the Sir2 family of NAD+-dependent histone/protein deacetylasesMargie T Borra
Department of Biomolecular Chemistry, University of Wisconsin, Madison, Wisconsin 53706 1532, USA
Biochemistry 43:9877-87. 2004The Silent information regulator 2 (Sir2) family of enzymes consists of NAD(+)-dependent histone/protein deacetylases that tightly couple the hydrolysis of NAD(+) and the deacetylation of an acetylated substrate to form nicotinamide, the ..
- Enhancing cell longevity for cosmetic application: a complementary approachMarielle Moreau
LVMH Recherche Parfums Christian Dior, St jean de braye, France
J Drugs Dermatol 6:s14-9. 2007..This study focuses on 1) yeast Kluyveromyces biopetides in stimulating the expression of sirtuin in human cutaneous cells and 2) the benefit for the skin of an active skin care product containing yeast Kluyveromyces biopetides...
- Mechanism-based inhibition of Sir2 deacetylases by thioacetyl-lysine peptideBrian C Smith
Department of Chemistry, University of Wisconsin, Madison, Wisconsin 53706 1532, USA
Biochemistry 46:14478-86. 2007..deacetylation reaction, the thioacetyl-lysine peptide exhibited exceptionally potent inhibition of sirtuins Sirt1, Sirt2, Sirt3, and Hst2...
- MEC1-dependent redistribution of the Sir3 silencing protein from telomeres to DNA double-strand breaksK D Mills
Massachusetts Institute of Technology, Department of Biology, Cambridge 02139, USA
Cell 97:609-20. 1999The yeast Sir2/3/4p complex is found in abundance at telomeres, where it participates in the formation of silent heterochromatin and telomere maintenance...
- DNA damage triggers disruption of telomeric silencing and Mec1p-dependent relocation of Sir3pA D McAinsh
Wellcome Trust Cancer Research Campaign Institute, Department of Zoology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QR, UK
Curr Biol 9:963-6. 1999..NHEJ also requires the SIR2, SIR3 and SIR4 gene products  , which are responsible for silencing at telomeres and the mating-type loci ...
- Acetyl-lysine analog peptides as mechanistic probes of protein deacetylasesBrian C Smith
Department of Chemistry, University of Wisconsin Madison, Madison, Wisconsin 53706 1532, USA
J Biol Chem 282:37256-65. 2007..tighter to Hst2 compared with acetyl-lysine peptide and showed measurable rates of catalysis with Hst2, Sirt1, Sirt2, and Sirt3, suggesting propionyl- and butyryl-lysine proteins may be sirtuin substrates in vivo...
- Sirtuins (histone deacetylases III) in the cellular response to DNA damage--facts and hypothesesMarcin Kruszewski
Department of Radiobiology and Health Protection, Institute of Nuclear Chemistry and Technology, Dorodna 16, 03 195 Warszawa, Poland
DNA Repair (Amst) 4:1306-13. 2005..Homologues of the yeast gene SIR2 in mammalian cells code type III histone deacetylases (HDAC III, sirtuins), dependent on NAD(+) and inhibited by ..
- Transition state of ADP-ribosylation of acetyllysine catalyzed by Archaeoglobus fulgidus Sir2 determined by kinetic isotope effects and computational approachesYana Cen
Department of Pharmacology, Weill Medical College of Cornell University, 1300 York Avenue, New York, New York 10065, USA
J Am Chem Soc 132:12286-98. 2010..A concerted yet highly asynchronous substitution mechanism forms the ADPR-peptidylimidate intermediate of the sirtuin deacetylation reaction...
- Sirtuins and their relevance to the kidneyChuan Ming Hao
Division of Nephrology and Hypertension, Vanderbilt University School of Medicine, Nashville, TN 37232, USA
J Am Soc Nephrol 21:1620-7. 2010Sirtuins (silent information regulator 2 [Sir2] proteins) belong to an ancient family of evolutionary conserved nicotinamide adenine dinucleotide (NAD)(+)-dependent enzymes with deacetylase and/or mono-ADP-ribosyltransferase activity...
- Crystal structure of a SIR2 homolog-NAD complexJ Min
W M Keck Structural Biology Laboratory, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA
Cell 105:269-79. 2001The SIR2 protein family comprises a novel class of nicotinamide-adenine dinucleotide (NAD)-dependent protein deacetylases that function in transcriptional silencing, DNA repair, and life-span extension in Saccharomyces cerevisiae...
- Conserved locus-specific silencing functions of Schizosaccharomyces pombe sir2+Lisa L Freeman-Cook
Division of Biological Sciences, Section of Molecular Biology and UCSD Center for Cancer Research, University of California, San Diego, 92093 0347, USA
Genetics 169:1243-60. 2005In Schizosaccharomyces pombe, three genes, sir2(+), hst2(+), and hst4(+), encode members of the Sir2 family of conserved NAD(+)-dependent protein deacetylases. The S...
- Linking sirtuins, IGF-I signaling, and starvationValter D Longo
Department of Biological Sciences, University of Southern California, 3715 McClintock Avenue, Los Angeles, CA 90089, USA
Exp Gerontol 44:70-4. 2009..Whereas other laboratories have proposed that sirtuins (Sir2 and its homologs), a family of conserved proteins which are NAD(+)-dependent histone deacetylases, can extend ..
- Mouse Sir2 homolog SIRT6 is a nuclear ADP-ribosyltransferaseGregory Liszt
Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA
J Biol Chem 280:21313-20. 2005Members of the Sir2 family of NAD-dependent protein deacetylases regulate diverse cellular processes including aging, gene silencing, and cellular differentiation...
- Mechanism of human SIRT1 activation by resveratrolMargie T Borra
Department of Biomolecular Chemistry, University of Wisconsin Madison, Madison, Wisconsin 53706, USA
J Biol Chem 280:17187-95. 2005..Among the three enzymes tested (yeast Sir2, human SIRT1, and human SIRT2), only SIRT1 exhibited significant enzyme activation ( approximately 8-fold) using the commercially available ..
- Sir2 regulates histone H3 lysine 9 methylation and heterochromatin assembly in fission yeastGurumurthy D Shankaranarayana
Cold Spring Harbor Laboratory, P O Box 100, Cold Spring Harbor, NY 11724, USA
Curr Biol 13:1240-6. 2003..budding yeast Saccharomyces cerevisiae, deacetylation of histones in heterochromatic chromosomal domains requires Sir2, a phylogenetically conserved NAD(+)-dependent deacetylase...
- Nicotinamide riboside and nicotinic acid riboside salvage in fungi and mammals. Quantitative basis for Urh1 and purine nucleoside phosphorylase function in NAD+ metabolismPeter Belenky
Department of Genetics and Biochemistry, Dartmouth Medical School, Lebanon, New Hampshire 03756, USA
J Biol Chem 284:158-64. 2009..substrate of ADP-ribose transfer enzymes and sirtuins, the type III protein lysine deacetylases related to yeast Sir2. Supplementation of yeast cells with nicotinamide riboside extends replicative lifespan and increases Sir2-..
- Sirtuin mechanism and inhibition: explored with N(ε)-acetyl-lysine analogsBrett M Hirsch
Department of Chemistry, University of Akron, 190 E Buchtel Commons, Akron, OH 44325, USA
Mol Biosyst 7:16-28. 2011b>Silent information regulator 2 (Sir2) enzymes or sirtuins are a family of intracellular protein deacetylases that can catalyze the β-nicotinamide adenine dinucleotide (β-NAD(+))-dependent deacetylation of N(ε)-acetyl-lysine on protein ..
- Analysis of O-acetyl-ADP-ribose as a target for Nudix ADP-ribose hydrolasesLouise A Rafty
Oregon Health and Science University, Department of Biochemistry and Molecular Biology, Portland, Oregon 97201 3098, USA
J Biol Chem 277:47114-22. 2002The Sir2 family of NAD(+)-dependent histone/protein deacetylases has been implicated in a wide range of biological activities, including gene silencing, life span extension, and chromosomal stability...
- Acetylation-dependent ADP-ribosylation by Trypanosoma brucei Sir2Terri M Kowieski
Department of Biomolecular Chemistry, University of Wisconsin, School of Medicine and Public Health, Madison, Wisconsin 53706, USA
J Biol Chem 283:5317-26. 2008..Here we explored the mechanisms of ADP-ribosylation using the Trypanosoma brucei Sir2 homologue TbSIR2rp1 as a model for sirtuins that reportedly display both activities...
- SIR2: the biochemical mechanism of NAD(+)-dependent protein deacetylation and ADP-ribosyl enzyme intermediatesAnthony A Sauve
Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Ave F304, Bronx, NY 10461, USA
Curr Med Chem 11:807-26. 2004The Sir2 family of enzymes is a recently described class of NAD(+)-dependent protein deacetylases that use NAD+ as a reactant to deacetylate acetyllysine residues of protein substrates to form the aminolysine sidechain and a novel product ..
- N(epsilon)-Modified lysine containing inhibitors for SIRT1 and SIRT2Tero Huhtiniemi
School of Pharmacy, University of Eastern Finland, Kuopio Campus, PO Box 1627, 70211 Kuopio, Finland
Bioorg Med Chem 18:5616-25. 2010..been used as a probe for the screening of novel N(epsilon)-modified lysine containing inhibitors against SIRT1 and SIRT2. N(epsilon)-Selenoacetyl and N(epsilon)-isothiovaleryl were the most potent moieties found in this study, ..
- Opposing effects of sirtuins on neuronal survival: SIRT1-mediated neuroprotection is independent of its deacetylase activityJason A Pfister
Department of Molecular and Cell Biology, University of Texas at Dallas, Richardson, TX, USA
PLoS ONE 3:e4090. 2008..Indeed, SIRT1 has been reported to protect against neuronal death, while SIRT2 promotes neurodegeneration...
- Chromosomal organization and fluorescence in situ hybridization of the human Sirtuin 6 geneUlrich Mahlknecht
Department of Hematology Oncology, University of Heidelberg Medical Center, D 69120 Heidelberg, Germany
Int J Oncol 28:447-56. 2006..Sirtuin 6 (SIRT6) is a member of the sirtuin deacetylases (sirtuins), which are derivatives of the yeast Silent information regulator 2 (Sir2) protein...
- Structural identification of 2'- and 3'-O-acetyl-ADP-ribose as novel metabolites derived from the Sir2 family of beta -NAD+-dependent histone/protein deacetylasesMichael D Jackson
Oregon Health and Science University, Department of Biochemistry and Molecular Biology, Portland, Oregopn 97201 3098, USA
J Biol Chem 277:18535-44. 2002The Sir2 (silent information regulator 2) family of histone/protein deacetylases has been implicated in a wide range of biological activities, including gene silencing, life-span extension, and chromosomal stability...
- "Clocks" in the NAD World: NAD as a metabolic oscillator for the regulation of metabolism and agingShin Ichiro Imai
Department of Developmental Biology, Washington University School of Medicine, St Louis, MO 63110, USA
Biochim Biophys Acta 1804:1584-90. 2010SIR2 (silent information regulator 2) proteins, now called "sirtuins," are an evolutionarily conserved family of NAD-dependent protein deacetylases/ADP-ribosyltransferases...
- Fluorescence in situ hybridization and chromosomal organization of the human Sirtuin 7 geneSusanne Voelter-Mahlknecht
Department of Hematology Oncology, University of Heidelberg Medical Center, D 69120 Heidelberg, Germany
Int J Oncol 28:899-908. 2006..is a member of the sirtuin family of protein deacetylases and is, therefore, a derivative of yeast Silent information regulator 2 (SIR2)...
- The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylasesJ Landry
Department of Biochemistry and Cell Biology, State University of New York, Stony Brook, NY 11794 5215, USA
Proc Natl Acad Sci U S A 97:5807-11. 2000Homologs of the chromatin-bound yeast silent information regulator 2 (SIR2) protein are found in organisms from all biological kingdoms...
- Sirtuin-targeting drugs: Mechanisms of action and potential therapeutic applicationsAhmad Aljada
Long Island University, Department of Biomedical Sciences, Brookville, NY 11548, USA
Curr Opin Investig Drugs 11:1158-68. 2010..sirtuins are NAD+-dependent histone/protein deacetylases that are similar to Saccharomyces cerevisiae silent information regulator 2 (Sir2)...
- Sirtuins: the 'magnificent seven', function, metabolism and longevityNassim Dali-Youcef
Institut de Génétique et de Biologie Moléculaire et Cellulaire de Strasbourg IGBMC, INSERM CNRS ULP, Illkirch, France
Ann Med 39:335-45. 2007..of histone deacetylases (HDACs) was named after their homology to the Saccharomyces cerevisiae gene silent information regulator 2 (Sir2)...
- A buoyancy-based screen of Drosophila larvae for fat-storage mutants reveals a role for Sir2 in coupling fat storage to nutrient availabilityTânia Reis
Department of Molecular and Cell Biology, University of California, Berkeley, California, United States of America
PLoS Genet 6:e1001206. 2010..Among these was a sirtuin family member, Sir2. Sirtuins regulate the storage and metabolism of carbohydrates and lipids by deacetylating key regulatory proteins...
- The 39-kDa poly(ADP-ribose) glycohydrolase ARH3 hydrolyzes O-acetyl-ADP-ribose, a product of the Sir2 family of acetyl-histone deacetylasesTohru Ono
Pulmonary Critical Care Medicine Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892 1590, USA
Proc Natl Acad Sci U S A 103:16687-91. 2006The silent information regulator 2 (Sir2) family of NAD-dependent N-acetyl-protein deacetylases participates in the regulation of gene silencing, chromatin structure, and longevity...
- Use of substrate analogs and mutagenesis to study substrate binding and catalysis in the Sir2 family of NAD-dependent protein deacetylasesAhlia N Khan
Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada
J Biol Chem 281:11702-11. 2006The Sir2 family of enzymes is highly conserved throughout evolution and functions in silencing, control of life span, apoptosis, and many other cellular processes...
- Sirtuin regulates cigarette smoke-induced proinflammatory mediator release via RelA/p65 NF-kappaB in macrophages in vitro and in rat lungs in vivo: implications for chronic inflammation and agingSe Ran Yang
Department of Environmental Medicine, Division of Lung Biology and Disease, University of Rochester Medical Center, MRBX 3 11106, 601 Elmwood Ave, Box 850, Rochester, NY 14642, USA
Am J Physiol Lung Cell Mol Physiol 292:L567-76. 2007The silent information regulator 2 (Sir2) family of proteins (sirtuins or SIRTs), which belong to class III histone/protein deacetylases, have been implicated in calorie restriction, aging, and inflammation...
- The Drosophila melanogaster sir2+ gene is nonessential and has only minor effects on position-effect variegationStefan U Aström
Department of Developmental Biology, Wennergren Institute, Stockholm University, SE 106 91 Stockholm, Sweden
Genetics 163:931-7. 2003Five Drosophila melanogaster genes belong to the highly conserved sir2 family, which encodes NAD(+)-dependent protein deacetylases...
- Sirtuins in mammals: insights into their biological functionShaday Michan
Department of Pathology, Paul F Glenn Laboratories for the Biological Mechanisms of Aging, Harvard Medical School, 77 Ave Louis Pasteur, Boston, MA, USA
Biochem J 404:1-13. 2007..Sirtuins are a conserved family of proteins found in all domains of life. The first known sirtuin, Sir2 (silent information regulator 2) of Saccharomyces cerevisiae, from which the family derives its name, regulates ribosomal DNA ..
- SIRT2 suppresses adipocyte differentiation by deacetylating FOXO1 and enhancing FOXO1's repressive interaction with PPARgammaFei Wang
USDA ARS Children s Nutrition Research Center, Department of Pediatrics, Baylor College of Medicine, Houston, TX 77030, USA
Mol Biol Cell 20:801-8. 2009..have previously reported that caloric restriction increases the expression of one of the seven mammalian sirtuins, SIRT2, in tissues such as white adipose tissue...
- Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylationDavid B Lombard
Howard Hughes Medical Institute, The Children s Hospital, Harvard Medical School, Boston, MA 02115, USA
Mol Cell Biol 27:8807-14. 2007Homologs of the Saccharomyces cerevisiae Sir2 protein, sirtuins, promote longevity in many organisms. Studies of the sirtuin SIRT3 have so far been limited to cell culture systems...
- SIRT2 regulates NF-κB dependent gene expression through deacetylation of p65 Lys310Karin M Rothgiesser
Institute of Veterinary Biochemistry and Molecular Biology, University of Zurich, Winterthurerstrase 190, 8057 Zurich, Switzerland
J Cell Sci 123:4251-8. 2010..In this study, we identified SIRT2 as a deacetylase of the transcription factor p65...
- Nuclear export modulates the cytoplasmic Sir2 homologue Hst2Jeanne M Wilson
Division of Biological Sciences, Section of Molecular Biology, University of California, San Diego, 9500 Gilman Drive, 0347, La Jolla, California 92093, USA
EMBO Rep 7:1247-51. 2006Modulating transcription factors is crucial to executing sophisticated gene expression programs. The silent information regulator 2 (Sir2) family of NAD-dependent protein deacetylases influences transcription by targeting proteins such as ..
- SirT1 inhibition reduces IGF-I/IRS-2/Ras/ERK1/2 signaling and protects neuronsYing Li
Neuroscience Program, University of Southern California, Los Angeles, CA 90089 2520, USA
Cell Metab 8:38-48. 2008Sirtuins are known to protect cells and extend life span, but our previous studies indicated that S. cerevisiae Sir2 can also increase stress sensitivity and limit life-span extension...
- Structural basis for the mechanism and regulation of Sir2 enzymesJose L Avalos
Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205 USA
Mol Cell 13:639-48. 2004b>Sir2 proteins form a family of NAD(+)-dependent protein deacetylases required for diverse biological processes, including transcriptional silencing, suppression of rDNA recombination, control of p53 activity, regulation of acetyl-CoA ..
- Genomewide screen for negative regulators of sirtuin activity in Saccharomyces cerevisiae reveals 40 loci and links to metabolismRyan M Raisner
Department of Biochemistry and Biophysics, University of California, San Francisco, California 94158 2200, USA
Genetics 179:1933-44. 2008..In Saccharomyces cerevisiae, the sirtuin Silent information regulator 2 (Sir2) promotes silent chromatin formation, suppresses recombination between repeats, and inhibits ..
- The role of sirtuins in the control of metabolic homeostasisJiujiu Yu
Institut de Genetique et de Biologie Moleculaire et Cellulaire, CNRS INSERM Université Louis Pasteur and Institut Clinique de la Souris, Illkirch, France
Ann N Y Acad Sci 1173:E10-9. 2009..the function of the sirtuin family, named after their homology to the Saccharomyces cerevisiae gene silent information regulator 2 (Sir2), has received a lot of attention, as their beneficial impact on longevity was linked to their ..
- Where in the cell is SIRT3?--functional localization of an NAD+-dependent protein deacetylaseWilliam C Hallows
Department of Biomolecular Chemistry, School of Medicine and Public Health, University of Wisconsin, Madison, WI 53706, USA
Biochem J 411:e11-3. 2008..SIRT3 (sirtuin 3), a human homologue of Sir2 (silent information regulator 2), has been genetically linked to lifespan in the elderly...
- Structure of a Sir2 enzyme bound to an acetylated p53 peptideJose L Avalos
Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA
Mol Cell 10:523-35. 2002b>Sir2 proteins are NAD(+)-dependent protein deacetylases that play key roles in transcriptional regulation, DNA repair, and life span regulation...
- Development and characterization of lysine based tripeptide analogues as inhibitors of Sir2 activitySubhra Prakash Chakrabarty
Molecular Biology and Genetics Unit, Jawaharlal Nehru Centre for Advanced Scientific Research, Jakkur, Bangalore 560064, India
Bioorg Med Chem 17:8060-72. 2009..protected lysine residues and their characterization as inhibitors of Plasmodiumfalciparum Sir2 activity...
- Histone H4 lysine 16 acetylation regulates cellular lifespanWeiwei Dang
Gene Expression and Regulation Program, The Wistar Institute Philadelphia, Pennsylvania 19104, USA
Nature 459:802-7. 2009..Yeast Sir2, the first member of the family to be found, establishes and maintains chromatin silencing by removing histone H4 ..
- Structure and substrate binding properties of cobB, a Sir2 homolog protein deacetylase from Escherichia coliKehao Zhao
The Wistar Institute, University of Pennsylvania, Philadelphia, PA 19104, USA
J Mol Biol 337:731-41. 2004..Together, these studies suggest that substrate-specific binding by sirtuin proteins involves contributions from the zinc-binding domain of the enzyme and substrate regions distal to the acetyl-lysine-binding site...
- Silent information regulator 2alpha, a longevity factor and class III histone deacetylase, is an essential endogenous apoptosis inhibitor in cardiac myocytesRalph R Alcendor
Cardiovascular Research Institute, Department of Cell Biology and Molecular Medicine, University of Medicine and Dentistry of New Jersey, New Jersey Medical School, Newark 07103, USA
Circ Res 95:971-80. 2004Yeast silent information regulator 2 (Sir2), a nicotinamide adenine dinucleotide-dependent histone deacetylase (HDAC) and founding member of the HDAC class III family, functions in a wide array of cellular processes, including gene ..
- A novel chalcone polyphenol inhibits the deacetylase activity of SIRT1 and cell growth in HEK293T cellsTomoaki Kahyo
Mitsubishi Kagaku Institute of Life Sciences MITILS, Machida, Tokyo, Japan
J Pharmacol Sci 108:364-71. 2008SIRT1 is one of seven mammalian orthologs of yeast silent information regulator 2 (Sir2), and it functions as a nicotinamide adenine dinucleotide (NAD)-dependent deacetylase...
- SIRT3, a human SIR2 homologue, is an NAD-dependent deacetylase localized to mitochondriaPatrick Onyango
Institute of Genetic Medicine, Department of Medicine, The Johns Hopkins University School of Medicine, 1064 Ross, 720 Rutland Avenue, Baltimore, MD 21205, USA
Proc Natl Acad Sci U S A 99:13653-8. 2002The SIR2 (silent information regulator 2) gene family has diverse functions in yeast including gene silencing, DNA repair, cell-cycle progression, and chromosome fidelity in meiosis and aging...
- A sirtuin in the African trypanosome is involved in both DNA repair and telomeric gene silencing but is not required for antigenic variationSam Alsford
London School of Hygiene and Tropical Medicine, Keppel Street, London, WC1E 7HT, UK
Mol Microbiol 63:724-36. 2007b>Silent information regulator 2 (Sir2)-related proteins or sirtuins function as NAD(+)-dependent deacetylases or ADP ribosylases that target a range of substrates, thereby influencing chromatin structure and a diverse range of other ..
- Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's diseaseTiago Fleming Outeiro
Alzheimer s Research Unit, MGH, Harvard Medical School, CNY 114, 16th Street, Charlestown, MA 02129, USA
Science 317:516-9. 2007..We identified a potent inhibitor of sirtuin 2 (SIRT2) and found that inhibition of SIRT2 rescued alpha-synuclein toxicity and modified inclusion morphology in ..
- Sirtuin-independent effects of nicotinamide on lifespan extension from calorie restriction in yeastMitsuhiro Tsuchiya
Department of Biochemistry, University of Washington, Seattle, WA 98195, USA
Aging Cell 5:505-14. 2006..longevity in yeast: (i) suppression of rDNA recombination through activation of the sirtuin protein deacetylase Sir2 or (ii) decreased activity of the nutrient-responsive kinases Sch9 and TOR...
- Omega-3 fatty acids supplementation restores mechanisms that maintain brain homeostasis in traumatic brain injuryAiguo Wu
Department of Physiological Science, University of California at Los Angeles UCLA, Los Angeles, California 90095, USA
J Neurotrauma 24:1587-95. 2007..The silent information regulator 2 (Sir2) has been implicated with maintaining genomic stability and cellular homeostasis under ..
- Replication fork arrest and rDNA silencing are two independent and separable functions of the replication terminator protein Fob1 of Saccharomyces cerevisiaeNarendra K Bairwa
Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, South Carolina 29425, USA
J Biol Chem 285:12612-9. 2010..Ter sites located in the intergenic spacer region of rDNA but also loads the NAD-dependent histone deacetylase Sir2 at Ter sites via a protein complex called RENT (regulator of nucleolar silencing and telophase exit)...
- HST1, a new member of the SIR2 family of genesM K Derbyshire
Gene Regulation and Chromosome Biology Laboratory, NCI Frederick Cancer Research and Development Center, ABL Basic Research Program, Maryland 21702 1201, USA
Yeast 12:631-40. 1996..HST1 is very closely related to SIR2, showing 71% sequence identity over 84% of its length. Polymerase chain reaction with degenerate primers on S...
- The deacetylase Sir2 from the yeast Clavispora lusitaniae lacks the evolutionarily conserved capacity to generate subtelomeric heterochromatinCara A Froyd
Biochemistry Department, Duke University, Durham, North Carolina, United States of America
PLoS Genet 9:e1003935. 2013Deacetylases of the Sir2 or sirtuin family are thought to regulate life cycle progression and life span in response to nutrient availability...
- Sirt2 suppresses glioma cell growth through targeting NF-κB-miR-21 axisYa Nan Li
Department of Neurosurgery, Changhai Hospital, Second Military Medical University, Shanghai, China
Biochem Biophys Res Commun 441:661-7. 2013..Here we report that Sir2 was under expressed in human glioma tissues and cell lines. We found that Sirt2 overexpression decreased cell proliferation and colony formation capacity...
- A unique class of conditional sir2 mutants displays distinct silencing defects in Saccharomyces cerevisiaeSandra N Garcia
Division of Biology, UCSD Cancer Center and Center for Molecular Genetics, University of California, San Diego 92093 0347, USA
Genetics 162:721-36. 2002..The NAD(+)-dependent deacetylation of histones by the Sir2p family of proteins lends mechanistic insight into how SIR2 contributes to silencing...
- Variability of the SIRT3 gene, human silent information regulator Sir2 homologue, and survivorship in the elderlyG Rose
Department of Cell Biology, University of Calabria, Rende 87030, Italy
Exp Gerontol 38:1065-70. 2003..a putative mitochondrial NAD-dependent deacetylase (SIRT3) which belongs to the evolutionary conserved family of sirtuin 2 proteins...
- Progressive loss of SIRT1 with cell cycle withdrawalTsutomu Sasaki
Department of Neuroscience, University of Virginia School of Medicine, Charlottesville, VA 22908, USA
Aging Cell 5:413-22. 2006b>Sir2 is an NAD+-dependent deacetylase that regulates lifespan in yeast, worms and flies. The mammalian orthologs of Sir2 include SIRT1 in humans and mice...
- [Functional analysis of SIR2]Yoshiyuki Horio
Department of Pharmacology, Sapporo Medical University, Sapporo 060 8556, Japan
Nihon Yakurigaku Zasshi 122:30P-32P. 2003The yeast silent information regulator 2 (Sir2) is an NAD-dependent histone deacetylase and silences transcription at the mating type loci, telomeres and the ribosomal DNA. Over-expression of Sir2 extends the life span of yeast and C...
- Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD(+)-dependent Sir2 histone/protein deacetylasesKehao Zhao
The Wistar Institute, Department of Biochemistry and Biophysics, School of Medicine, and Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104
Proc Natl Acad Sci U S A 101:8563-8. 2004b>Sir2 enzymes are broadly conserved from bacteria to humans and have been implicated to play roles in gene silencing, DNA repair, genome stability, longevity, metabolism, and cell physiology...
- Altered expression of SIRT gene family in head and neck squamous cell carcinomaChi Chih Lai
Division of Laryngology, Department of Otolaryngology, Kaohsiung Chang Gung Memorial Hospital, Chang Gung University College of Medicine, 123 Da Pi Rd, Niaosong District, 833 Kaohsiung City, Taiwan
Tumour Biol 34:1847-54. 2013..Our results demonstrated that the expression levels of SIRT1, SIRT2, SIRT3, SIRT5, SIRT6, and SIRT7 were significantly downregulated in cancerous tissues compared with noncancerous ..
- Silent information regulator 2 potentiates Foxo1-mediated transcription through its deacetylase activityHiroaki Daitoku
Center for Tsukuba Advanced Research Alliance, University of Tsukuba, 1 1 1 Ten noudai, Tsukuba, Ibaraki 305 8577, Japan
Proc Natl Acad Sci U S A 101:10042-7. 2004..genes include the Forkhead transcription factor FOXO and the NAD-dependent histone deacetylase silent information regulator 2 (Sir2)...
- Small molecule regulation of Sir2 protein deacetylasesOlivera Grubisha
Department of Biomolecular Chemistry, University of Wisconsin, Madison, WI 53706 1532, USA
FEBS J 272:4607-16. 2005The Sir2 family of histone/protein deacetylases (sirtuins) is comprised of homologues found across all kingdoms of life...
- Phosphorylation regulates SIRT1 functionTsutomu Sasaki
Neuroscience Graduate Program, University of Virginia, Charlottesville, Virginia, United States of America
PLoS ONE 3:e4020. 2008b>SIR2 is an NAD(+)-dependent deacetylase - implicated in the regulation of lifespan in species as diverse as yeast , worms , and flies ...
- Drosophila Sir2 is required for heterochromatic silencing and by euchromatic Hairy/E(Spl) bHLH repressors in segmentation and sex determinationMiriam I Rosenberg
Division of Basic Sciences and Program in Developmental Biology, Fred Hutchinson Cancer Research Center, Seattle, WA 98109, USA
Cell 109:447-58. 2002Yeast SIR2 is a NAD+-dependent histone deacetylase required for heterochromatic silencing at telomeres, rDNA, and mating-type loci...
- Mechanism-based modulator discovery for sirtuin-catalyzed deacetylation reactionWeiping Zheng
School of Pharmacy, Jiangsu University, Zhenjiang 212013, P R China
Mini Rev Med Chem 13:132-54. 2013b>Silent information regulator 2 (Sir2) enzymes or sirtuins are a family of evolutionarily conserved intracellular protein deacetylases that can catalyze the acetyl group removal from the specific Nε-acetyl-lysine (AcK) side chains on a ..
- Tenovin-D3, a novel small-molecule inhibitor of sirtuin SirT2, increases p21 (CDKN1A) expression in a p53-independent mannerAnna R McCarthy
Department of Microbiology, Tumor and Cell Biology, Karolinska Institutet, Stockholm, Sweden
Mol Cancer Ther 12:352-60. 2013..Recent studies show that tenovin-6, a small-molecule inhibitor of sirtuins SirT1 and SirT2, reduces tumor growth in vivo and eliminates leukemic stem cells in a murine model for chronic myelogenous ..
- Poly(ADP-ribose) polymerase mediates both cell death and ATP decreases in SIRT2 inhibitor AGK2-treated microglial BV2 cellsYexin Li
School of Biomedical Engineering and Med X Research Institute, Shanghai Jiao Tong University, Shanghai 200030, PR China
Neurosci Lett 544:36-40. 2013b>Sirtuin 2 (SIRT2), a sirtuin family protein, is a tubulin deacetylase...
- Splitomicin inhibits fMLP-induced superoxide anion production in human neutrophils by activate cAMP/PKA signaling inhibition of ERK pathwayFu Chao Liu
Department of Anesthesiology, Chang Gung Memorial Hospital, Linkou, Taiwan, ROC
Eur J Pharmacol 688:68-75. 2012..a cell-permeable lactone derived from naphthol and known to be a potent selective inhibitor of Sir2 (silent information regulator 2)...
- Design, synthesis, and biological activity of a novel series of human sirtuin-2-selective inhibitorsTakayoshi Suzuki
Graduate School of Medical Science, Kyoto Prefectural University of Medicine, 13 Taishogun Nishitakatsukasa cho, Kita ku, Kyoto 603 8334, Japan
J Med Chem 55:5760-73. 2012Selective inhibitors of human sirtuin 2 (SIRT2), a deacetylase, are candidate therapeutic agents for neurodegenerative diseases such as Parkinson's disease and Huntington's disease as well as potential tools for elucidating the ..
- Molecular modeling study for conformational changes of Sirtuin 2 due to substrate and inhibitor bindingSugunadevi Sakkiah
Division of Applied Life Science BK21 program, Systems and Synthetic Agrobiotech Center SSAAC, Gyeongsang National University GNU, Gazha dong, Jinju, Republic of Korea
J Biomol Struct Dyn 30:235-54. 2012Sirtuin is a member of NAD(+)-dependent deacetylase family. The structural details of Sirtuin 2 (SIRT2) complex will be very useful to discover the drug which might have beneficial effects on various diseases like cancer, diabetes, etc...
- Molecular docking and dynamics simulation, receptor-based hypothesis: application to identify novel sirtuin 2 inhibitorsSugunadevi Sakkiah
Division of Applied Life Science BK21 program, Systems and Synthetic Agrobiotech Center SSAC, Plant Molecular Biology and Biotechnology Research Center PMBBRC, Research Institute of Natural Science RINS, Gyeongsang National University GNU, 501 Jinju daero, Gazha dong, Jinju 660 701, Korea
Chem Biol Drug Des 80:315-27. 2012..Owing to the absence of complex structure of sirtuin 2 (SIRT2), sirtinol was docked in the NAD(+) binding site and subjected to 5-nseconds molecular dynamics (MD) ..
- Nicotinamide inhibits growth of carcinogen induced mouse bladder tumor and human bladder tumor xenograft through up-regulation of RUNX3 and p300Wun Jae Kim
Institute for Tumor Research and Department of Urology, College of Medicine, Cheongju, South Korea
J Urol 185:2366-75. 2011..We noted that the tumor suppressor RUNX3 is inactivated by promoter hypermethylation in human bladder cancer. We investigated whether reactivation of RUNX3 could suppress bladder cancer development in an animal model...
- Human Sir2-related protein SIRT1 associates with the bHLH repressors HES1 and HEY2 and is involved in HES1- and HEY2-mediated transcriptional repressionTakehiko Takata
Laboratory of Molecular and Cellular Assembly, Department of Biological Information, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta, Midori ku, Yokohama 226 8501, Japan
Biochem Biophys Res Commun 301:250-7. 2003..bHLH repressor proteins, Hairy and Deadpan, bind to and function with the NAD(+)-dependent histone deacetylase, Sir2. Here we demonstrate that the human Sir2 homologue, SIRT1, also physically associates with the human bHLH repressor ..
- Dietary obesity-associated Hif1α activation in adipocytes restricts fatty acid oxidation and energy expenditure via suppression of the Sirt2-NAD+ systemJaya Krishnan
Institute of Cell Biology, ETH Zurich, Switzerland
Genes Dev 26:259-70. 2012..of Hif1α is linked to its capacity to suppress β-oxidation, in part, through transcriptional repression of sirtuin 2 (Sirt2) NAD(+)-dependent deacetylase...
- Deacetylation of FOXO3 by SIRT1 or SIRT2 leads to Skp2-mediated FOXO3 ubiquitination and degradationF Wang
Children s Nutrition Research Center, Baylor College of Medicine, Houston, TX 77030, USA
Oncogene 31:1546-57. 2012..SIRT1 and SIRT2 deacetylate FOXO factors to regulate FOXO function...
- Sir2 is induced by oxidative stress in a yeast model of Huntington disease and its activation reduces protein aggregationM Alba Sorolla
Departament de Ciencies Mediques Basiques, IRBLLEIDA, Universitat de Lleida, Facultat de Medicina, Spain
Arch Biochem Biophys 510:27-34. 2011..Oxidative stress, either endogenous as a result of mutant polyQ expression or exogenously generated, increases Sir2 levels...
- Sir2 deletion prevents lifespan extension in 32 long-lived mutantsJoe R Delaney
Department of Pathology, University of Washington, Seattle, WA, USA
Aging Cell 10:1089-91. 2011Activation of Sir2 orthologs is proposed to increase lifespan downstream of dietary restriction...
- A possibility of nutriceuticals as an anti-aging intervention: activation of sirtuins by promoting mammalian NAD biosynthesisShin Ichiro Imai
Department of Developmental Biology, Washington University School of Medicine, Campus Box 8103, 660 South Euclid Avenue, St Louis, MO 63110, USA
Pharmacol Res 62:42-7. 2010..One potential target for the development of anti-aging drugs is the SIR2 (silent information regulator 2) family of NAD-dependent deacetylases/ADP-ribosyltransferases, called "sirtuins...
- Structure-based development of novel sirtuin inhibitorsChristine Schlicker
Department of Biophysics, Ruhr University Bochum, Germany
Aging (Albany NY) 3:852-72. 2011..Virtual docking of a compound library into the peptide binding pockets of crystal structures of Sirt2, 3, 5 and 6 yielded compounds potentially discriminating between these isoforms...
- The contribution of Toll-like receptor 2 to the innate recognition of a Leishmania infantum silent information regulator 2 proteinRicardo Silvestre
Parasite Disease Group, Instituto de Biologia Molecular e Celular, Universidade do Porto, Porto, Portugal
Immunology 128:484-99. 2009We have characterized a Leishmania protein belonging to the silent information regulator 2 (SIR2) family [SIR2 related protein 1 (SIR2RP1)] that might play an immunoregulatory role during infection through its capacity to trigger B-cell ..
- Protein Acetylation Signature of ES Cell DifferentiationAlexey Terskikh; Fiscal Year: 2007..In particular, we speculate that protein deacetylation mediated by the members of Sir2 family (mediated by the intracellular redox state) regulates the stem cell self-renewal vs...
- TRANSCRIPTIONAL SILENCING MECHANISMSJEF BOEKE; Fiscal Year: 2005..The Sir2 protein is required for all forms of silencing, while Sir3 and Sir4 are required for telomeric and HM loci ..
- Mechanism of Sir2 Family of NAD+-dependent DeacetylasesMargie Borra; Fiscal Year: 2005The silent information regulator 2 (Sir2) family of enzymes is conserved in organisms ranging from some bacteria to human...
- TWO NOVEL CPLA2 BINDING PROTEINS AND CELL DEATHJOSEPH VINCENT BONVENTRE; Fiscal Year: 2010..phospholipase A2 interacts with 3 proteins, including Tip60, a Tip60 splice variant which we have called PLIP, and SIRT2. The goals of this grant have been to study the molecular basis for and roles of these proteins in mesangial cell ..
- Sir2 regulation and chemical modulationAnthony A Sauve; Fiscal Year: 2010..abstract_text> ..
- Biochemical and genomic studies of histone deacetylasesBRADLEY BERNSTEIN; Fiscal Year: 2006..The yeast HDACs RPD3 and SIR2 have previously been shown to have opposite effects on silencing and aging...
- NAD+ control of transcriptional silencing and longevityDavid Sinclair; Fiscal Year: 2007..Yeast cells suppress this instability by forming "silent" heterochromatin at the rDNA locus. This process requires Sir2, an NAD+-dependent histone deacetylase...
- Discovery of genes that extend yeast lifespan: Aging in immobilized cell reactorsRAPHAEL ROSENZWEIG; Fiscal Year: 2009..studies using yeast have led to the discovery of the role played by the silent information regulator protein Sir2 in modulating replicative lifespan, and the roles played by Ras2, Cyr1 and Sch9 in modulating chronological ..