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词条 Sirtuin 2
释义

  1. Function

  2. Structure

      Gene    Protein  

  3. Selective ligands

      Inhibitors  

  4. Model organisms

  5. Animal studies

      Metabolic actions    Neurodegeneration  

  6. Clinical significance

     Metabolic actions  Cell cycle regulation   Tumorigenesis  

  7. Interactions

  8. References

  9. Further reading

{{Infobox_gene}}NAD-dependent deacetylase sirtuin 2 is an enzyme that in humans is encoded by the SIRT2 gene.[1][2][3] SIRT2 is an NAD+ (nicotinamide adenine dinucleotide)-dependent deacetylase. Studies of this protein have often been divergent, highlighting the dependence of pleiotropic effects of SIRT2 on cellular context. The natural polyphenol resveratrol is known to exert opposite actions on neural cells according to their normal or cancerous status.[4] Similar to other sirtuin family members, SIRT2 displays a ubiquitous distribution. SIRT2 is expressed in a wide range of tissues and organs and has been detected particularly in metabolically relevant tissues, including the brain, muscle, liver, testes, pancreas, kidney, and adipose tissue of mice. Of note, SIRT2 expression is much higher in the brain than all other organs studied, particularly in the cortex, striatum, hippocampus, and spinal cord.[5]

Function

Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity.[3] Cytosolic functions of SIRT2 include the regulation of microtubule acetylation, control of myelination in the central and peripheral nervous system{{Citation needed|reason= The citation at the end of this sentence does not address myelination in the central or peripheral nervous system.|date=June 2017}} and gluconeogenesis.[6] There is growing evidence for additional functions of SIRT2 in the nucleus. During the G2/M transition, nuclear SIRT2 is responsible for global deacetylation of H4K16, facilitating H4K20 methylation and subsequent chromatin compaction.[7] In response to DNA damage, SIRT2 was also found to deacetylate H3K56 in vivo.[8] Finally, SIRT2 negatively regulates the acetyltransferase activity of the transcriptional co-activator p300 via deacetylation of an automodification loop within its catalytic domain.[9]

Structure

Gene

Human SIRT2 gene has 18 exons resides on chromosome 19 at q13.[3] For SIRT2, four different human splice variants are deposited in the GenBank sequence database.[10]

Protein

SIRT2 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 protein encoded by this gene is included in class I of the sirtuin family. Several transcript variants are resulted from alternative splicing of this gene.[3] Only transcript variants 1 and 2 have confirmed protein products of physiological relevance. A leucine-rich nuclear export signal (NES) within the N-terminal region of these two isoforms is identified.[10] Since deletion of the NES led to nucleocytoplasmic distribution, it is suggested to mediate their cytosolic localization.[11]

Selective ligands

Inhibitors

  • Benzamide compound # 64[12]
  • (S)-2-Pentyl-6-chloro,8-bromo-chroman-4-one: IC50 of 1.5 μM, highly selective over SIRT2 and SIRT3[13]
  • 3′-Phenethyloxy-2-anilinobenzamide (33i): IC50 of 0.57 μM[14]

Model organisms

The functions of human sirtuins have not yet been determined; however, model organisms have been used in the study of SIRT2 function. Yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA.

A conditional knockout mouse line, called Sirt2tm1a(EUCOMM)Wtsi[16][17] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists — at the Wellcome Trust Sanger Institute.[18][19][20] Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[15][21]

Twenty five tests were carried out on homozygous mutant adult mice, however no significant abnormalities were observed.[15]

Animal studies

Metabolic actions

SIRT2 suppresses inflammatory responses in mice through p65 deacetylation and inhibition of NF-κB activity.[22] SIRT2 is responsible for the deacetylation and activation of G6PD, stimulating pentose phosphate pathway to supply cytosolic NADPH to counteract oxidative damage and protect mouse erythrocytes.[23]

Neurodegeneration

Several studies in cell and invertebrate models of Parkinson's disease (PD) and Huntington's disease (HD) suggested potential neuroprotective effects of SIRT2 inhibition, in striking contrast with other sirtuin family members.[24][25] In addition, recent evidence shows that inhibition of SIRT2 protects against MPTP-induced neuronal loss in vivo.[26]

Clinical significance

Metabolic actions

Several SIRT2 deacetylation targets play important roles in metabolic homeostasis. SIRT2 inhibits adipogenesis by deacetylating FOXO1 and thus may protect against insulin resistance. SIRT2 sensitizes cells to the action of insulin by physically interacting with and activating Akt and downstream targets. SIRT2 mediates mitochondrial biogenesis by deacetylating PGC-1α, upregulates antioxidant enzyme expression by deacetylating FOXO3a, and thereby reduces ROS levels.

Cell cycle regulation

Although preferentially cytosolic, SIRT2 transiently shuttles to the nucleus during the G2/M transition of the cell cycle, where it has a strong preference for histone H4 lysine 16 (H4K16Ac),[27] thereby regulating chromosomal condensation during mitosis.[28] During the cell cycle, SIRT2 associates with several mitotic structures including the centrosome, mitotic spindle, and midbody, presumably to ensure normal cell division.[11] Finally, cells with SIRT2 overexpression exhibit marked prolongation of the cell cycle.[29]

Tumorigenesis

Mounting evidence implies a role for SIRT2 in tumorigenesis. SIRT2 may suppress or promote tumor growth in a context-dependent manner. SIRT2 has been proposed to act as a tumor suppressor by preventing chromosomal instability during mitosis.[30] SIRT2-specific inhibitors exhibits broad anticancer activity.[31][32]

Interactions

SIRT2 has been shown to interact with:

  • α-tubulin,[33]
  • TUG,[34]
  • β-catenin,[35]
  • PGAM2,[36]
  • TIAM1,[37]
  • ApoE4,[38]
  • p53,[39]
  • PEPCK,[40]
  • FOXO1,[41]
  • p300,[42]
  • 14-3-3 protein,[43]
  • G6PD,[23][32] and
  • CBP.[44]

References

1. ^{{cite journal | vauthors = Afshar G, Murnane JP | title = Characterization of a human gene with sequence homology to Saccharomyces cerevisiae SIR2 | journal = Gene | volume = 234 | issue = 1 | pages = 161–68 | date = Jun 1999 | pmid = 10393250 | pmc = | doi = 10.1016/S0378-1119(99)00162-6 }}
2. ^{{cite journal | vauthors = Frye RA | title = Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity | journal = Biochemical and Biophysical Research Communications | volume = 260 | issue = 1 | pages = 273–79 | date = Jun 1999 | pmid = 10381378 | pmc = | doi = 10.1006/bbrc.1999.0897 }}
3. ^1 2 3 {{cite web | title = Entrez Gene: SIRT2 sirtuin (silent mating type information regulation 2 homolog) 2 (S. cerevisiae)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=22933| accessdate = }}
4. ^{{cite journal | vauthors = Sayd S, Junier MP, Chneiweiss H | title = [SIRT2, a multi-talented deacetylase] | journal = Médecine Sciences | volume = 30 | issue = 5 | pages = 532–36 | date = May 2014 | pmid = 24939540 | doi = 10.1051/medsci/20143005016 }}
5. ^{{cite journal | vauthors = Maxwell MM, Tomkinson EM, Nobles J, Wizeman JW, Amore AM, Quinti L, Chopra V, Hersch SM, Kazantsev AG | title = The Sirtuin 2 microtubule deacetylase is an abundant neuronal protein that accumulates in the aging CNS | journal = Human Molecular Genetics | volume = 20 | issue = 20 | pages = 3986–96 | date = Oct 2011 | pmid = 21791548 | doi = 10.1093/hmg/ddr326 | pmc=3203628}}
6. ^{{cite journal | vauthors = North BJ, Marshall BL, Borra MT, Denu JM, Verdin E | title = The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase | journal = Molecular Cell | volume = 11 | issue = 2 | pages = 437–44 | date = Feb 2003 | pmid = 12620231 | doi=10.1016/s1097-2765(03)00038-8}}
7. ^{{cite journal | vauthors = Serrano L, Martínez-Redondo P, Marazuela-Duque A, Vazquez BN, Dooley SJ, Voigt P, Beck DB, Kane-Goldsmith N, Tong Q, Rabanal RM, Fondevila D, Muñoz P, Krüger M, Tischfield JA, Vaquero A | title = The tumor suppressor SirT2 regulates cell cycle progression and genome stability by modulating the mitotic deposition of H4K20 methylation | journal = Genes & Development | volume = 27 | issue = 6 | pages = 639–53 | date = Mar 2013 | pmid = 23468428 | doi = 10.1101/gad.211342.112 | pmc=3613611}}
8. ^{{cite journal | vauthors = Vempati RK, Jayani RS, Notani D, Sengupta A, Galande S, Haldar D | title = p300-mediated acetylation of histone H3 lysine 56 functions in DNA damage response in mammals | journal = The Journal of Biological Chemistry | volume = 285 | issue = 37 | pages = 28553–64 | date = Sep 2010 | pmid = 20587414 | doi = 10.1074/jbc.M110.149393 | pmc=2937881}}
9. ^{{cite journal | vauthors = Black JC, Mosley A, Kitada T, Washburn M, Carey M | title = The SIRT2 deacetylase regulates autoacetylation of p300 | journal = Molecular Cell | volume = 32 | issue = 3 | pages = 449–55 | date = Nov 2008 | pmid = 18995842 | doi = 10.1016/j.molcel.2008.09.018 | pmc=2645867}}
10. ^1 {{cite journal | vauthors = Rack JG, VanLinden MR, Lutter T, Aasland R, Ziegler M | title = Constitutive nuclear localization of an alternatively spliced sirtuin-2 isoform | journal = Journal of Molecular Biology | volume = 426 | issue = 8 | pages = 1677–91 | date = Apr 2014 | pmid = 24177535 | doi = 10.1016/j.jmb.2013.10.027 }}
11. ^1 {{cite journal | vauthors = North BJ, Verdin E | title = Interphase nucleo-cytoplasmic shuttling and localization of SIRT2 during mitosis | journal = PLOS One | volume = 2 | issue = 8 | page = e784 | date = 29 August 2007 | pmid = 17726514 | doi = 10.1371/journal.pone.0000784 | pmc=1949146| bibcode = 2007PLoSO...2..784N }}
12. ^{{cite journal | vauthors = Cui H, Kamal Z, Ai T, Xu Y, More SS, Wilson DJ, Chen L | title = Discovery of potent and selective sirtuin 2 (SIRT2) inhibitors using a fragment-based approach | journal = Journal of Medicinal Chemistry | volume = 57 | issue = 20 | pages = 8340–57 | date = Oct 2014 | pmid = 25275824 | doi = 10.1021/jm500777s }}
13. ^{{cite journal | vauthors = Fridén-Saxin M, Seifert T, Landergren MR, Suuronen T, Lahtela-Kakkonen M, Jarho EM, Luthman K | title = Synthesis and evaluation of substituted chroman-4-one and chromone derivatives as sirtuin 2-selective inhibitors | journal = Journal of Medicinal Chemistry | volume = 55 | issue = 16 | pages = 7104–13 | date = Aug 2012 | pmid = 22746324 | pmc = 3426190 | doi = 10.1021/jm3005288 }}
14. ^{{cite journal | vauthors = Suzuki T, Khan MN, Sawada H, Imai E, Itoh Y, Yamatsuta K, Tokuda N, Takeuchi J, Seko T, Nakagawa H, Miyata N | title = Design, synthesis, and biological activity of a novel series of human sirtuin-2-selective inhibitors | journal = Journal of Medicinal Chemistry | volume = 55 | issue = 12 | pages = 5760–73 | date = Jun 2012 | pmid = 22642300 | doi = 10.1021/jm3002108 }}
15. ^1 2 {{cite journal| doi = 10.1111/j.1755-3768.2010.4142.x| title = The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice| year = 2010| author = Gerdin AK| journal = Acta Ophthalmologica| volume = 88| issue = S248 | pages = 0}}
16. ^{{cite web |url=http://www.knockoutmouse.org/martsearch/search?query=Sirt2 |title=International Knockout Mouse Consortium}}
17. ^{{cite web |url=http://www.informatics.jax.org/searchtool/Search.do?query=MGI:4431586 |title=Mouse Genome Informatics}}
18. ^{{cite journal | vauthors = Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A | title = A conditional knockout resource for the genome-wide study of mouse gene function | journal = Nature | volume = 474 | issue = 7351 | pages = 337–42 | date = Jun 2011 | pmid = 21677750 | pmc = 3572410 | doi = 10.1038/nature10163 }}
19. ^{{cite journal | vauthors = Dolgin E | title = Mouse library set to be knockout | journal = Nature | volume = 474 | issue = 7351 | pages = 262–63 | date = Jun 2011 | pmid = 21677718 | doi = 10.1038/474262a }}
20. ^{{cite journal | vauthors = Collins FS, Rossant J, Wurst W | title = A mouse for all reasons | journal = Cell | volume = 128 | issue = 1 | pages = 9–13 | date = Jan 2007 | pmid = 17218247 | doi = 10.1016/j.cell.2006.12.018 }}
21. ^{{cite journal | vauthors = van der Weyden L, White JK, Adams DJ, Logan DW | title = The mouse genetics toolkit: revealing function and mechanism | journal = Genome Biology | volume = 12 | issue = 6 | page = 224 | year = 2011 | pmid = 21722353 | pmc = 3218837 | doi = 10.1186/gb-2011-12-6-224 }}
22. ^{{cite journal | vauthors = Gomes P, Outeiro TF, Cavadas C | title = Emerging Role of Sirtuin 2 in the Regulation of Mammalian Metabolism | journal = Trends in Pharmacological Sciences | volume = 36 | issue = 11 | pages = 756–68 | date = Nov 2015 | pmid = 26538315 | doi = 10.1016/j.tips.2015.08.001 }}
23. ^1 {{cite journal | vauthors = Wang YP, Zhou LS, Zhao YZ, Wang SW, Chen LL, Liu LX, Ling ZQ, Hu FJ, Sun YP, Zhang JY, Yang C, Yang Y, Xiong Y, Guan KL, Ye D | title = Regulation of G6PD acetylation by SIRT2 and KAT9 modulates NADPH homeostasis and cell survival during oxidative stress | journal = The EMBO Journal | volume = 33 | issue = 12 | pages = 1304–20 | date = Jun 2014 | pmid = 24769394 | doi = 10.1002/embj.201387224 | pmc=4194121}}
24. ^{{cite journal | vauthors = Outeiro TF, Kontopoulos E, Altmann SM, Kufareva I, Strathearn KE, Amore AM, Volk CB, Maxwell MM, Rochet JC, McLean PJ, Young AB, Abagyan R, Feany MB, Hyman BT, Kazantsev AG | title = Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's disease | journal = Science | volume = 317 | issue = 5837 | pages = 516–19 | date = Jul 2007 | pmid = 17588900 | doi = 10.1126/science.1143780 | bibcode = 2007Sci...317..516O }}
25. ^{{cite journal | vauthors = Luthi-Carter R, Taylor DM, Pallos J, Lambert E, Amore A, Parker A, Moffitt H, Smith DL, Runne H, Gokce O, Kuhn A, Xiang Z, Maxwell MM, Reeves SA, Bates GP, Neri C, Thompson LM, Marsh JL, Kazantsev AG | title = SIRT2 inhibition achieves neuroprotection by decreasing sterol biosynthesis | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 107 | issue = 17 | pages = 7927–32 | date = Apr 2010 | pmid = 20378838 | doi = 10.1073/pnas.1002924107 | pmc=2867924| bibcode = 2010PNAS..107.7927L }}
26. ^{{cite journal | vauthors = Chen X, Wales P, Quinti L, Zuo F, Moniot S, Herisson F, Rauf NA, Wang H, Silverman RB, Ayata C, Maxwell MM, Steegborn C, Schwarzschild MA, Outeiro TF, Kazantsev AG | title = The sirtuin-2 inhibitor AK7 is neuroprotective in models of Parkinson's disease but not amyotrophic lateral sclerosis and cerebral ischemia | journal = PLOS One | volume = 10 | issue = 1 | page = e0116919 | date = 2015 | pmid = 25608039 | doi = 10.1371/journal.pone.0116919 | pmc=4301865| bibcode = 2015PLoSO..1016919C }}
27. ^{{cite journal | vauthors = Vaquero A, Scher MB, Lee DH, Sutton A, Cheng HL, Alt FW, Serrano L, Sternglanz R, Reinberg D | title = SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis | journal = Genes & Development | volume = 20 | issue = 10 | pages = 1256–61 | date = May 2006 | pmid = 16648462 | doi = 10.1101/gad.1412706 | pmc=1472900}}
28. ^{{cite journal | vauthors = Inoue T, Hiratsuka M, Osaki M, Yamada H, Kishimoto I, Yamaguchi S, Nakano S, Katoh M, Ito H, Oshimura M | title = SIRT2, a tubulin deacetylase, acts to block the entry to chromosome condensation in response to mitotic stress | journal = Oncogene | volume = 26 | issue = 7 | pages = 945–57 | date = Feb 2007 | pmid = 16909107 | doi = 10.1038/sj.onc.1209857 }}
29. ^{{cite journal | vauthors = Dryden SC, Nahhas FA, Nowak JE, Goustin AS, Tainsky MA | title = Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle | journal = Molecular and Cellular Biology | volume = 23 | issue = 9 | pages = 3173–85 | date = May 2003 | pmid = 12697818 | doi=10.1128/mcb.23.9.3173-3185.2003 | pmc=153197}}
30. ^{{cite journal | vauthors = Kim HS, Vassilopoulos A, Wang RH, Lahusen T, Xiao Z, Xu X, Li C, Veenstra TD, Li B, Yu H, Ji J, Wang XW, Park SH, Cha YI, Gius D, Deng CX | title = SIRT2 maintains genome integrity and suppresses tumorigenesis through regulating APC/C activity | journal = Cancer Cell | volume = 20 | issue = 4 | pages = 487–99 | date = Oct 2011 | pmid = 22014574 | doi = 10.1016/j.ccr.2011.09.004 | pmc=3199577}}
31. ^{{cite journal | vauthors = Jing H, Hu J, He B, Negrón Abril YL, Stupinski J, Weiser K, Carbonaro M, Chiang YL, Southard T, Giannakakou P, Weiss RS, Lin H | title = A SIRT2-Selective Inhibitor Promotes c-Myc Oncoprotein Degradation and Exhibits Broad Anticancer Activity | journal = Cancer Cell | volume = 29 | issue = 5 | pages = 767–68 | date = May 2016 | pmid = 27165747 | doi = 10.1016/j.ccell.2016.04.005 | access-date = | pmc = 4811675 }}
32. ^1 {{cite journal | vauthors = Xu SN, Wang TS, Li X, Wang YP | title = SIRT2 activates G6PD to enhance NADPH production and promote leukaemia cell proliferation | journal = Sci Rep | volume = 6 | page = 32734| date = Sep 2016 | pmid = 27586085 | doi = 10.1038/srep32734 | pmc=5009355| bibcode = 2016NatSR...632734X }}
33. ^{{cite journal | vauthors = Yuan Q, Zhan L, Zhou QY, Zhang LL, Chen XM, Hu XM, Yuan XC | title = SIRT2 regulates microtubule stabilization in diabetic cardiomyopathy | journal = European Journal of Pharmacology | volume = 764 | pages = 554–61 | date = Oct 2015 | pmid = 26209361 | doi = 10.1016/j.ejphar.2015.07.045 }}
34. ^{{cite journal | vauthors = Belman JP, Bian RR, Habtemichael EN, Li DT, Jurczak MJ, Alcázar-Román A, McNally LJ, Shulman GI, Bogan JS | title = Acetylation of TUG protein promotes the accumulation of GLUT4 glucose transporters in an insulin-responsive intracellular compartment | journal = The Journal of Biological Chemistry | volume = 290 | issue = 7 | pages = 4447–63 | date = Feb 2015 | pmid = 25561724 | pmc = 4326849 | doi = 10.1074/jbc.M114.603977 }}
35. ^{{cite journal | vauthors = Nguyen P, Lee S, Lorang-Leins D, Trepel J, Smart DK | title = SIRT2 interacts with β-catenin to inhibit Wnt signaling output in response to radiation-induced stress | journal = Molecular Cancer Research | volume = 12 | issue = 9 | pages = 1244–53 | date = Sep 2014 | pmid = 24866770 | doi = 10.1158/1541-7786.MCR-14-0223-T | pmc=4163538}}
36. ^{{cite journal | vauthors = Xu Y, Li F, Lv L, Li T, Zhou X, Deng CX, Guan KL, Lei QY, Xiong Y | title = Oxidative stress activates SIRT2 to deacetylate and stimulate phosphoglycerate mutase | journal = Cancer Research | volume = 74 | issue = 13 | pages = 3630–42 | date = Jul 2014 | pmid = 24786789 | doi = 10.1158/0008-5472.CAN-13-3615 | pmc=4303242}}
37. ^{{cite journal | vauthors = Saxena M, Dykes SS, Malyarchuk S, Wang AE, Cardelli JA, Pruitt K | title = The sirtuins promote Dishevelled-1 scaffolding of TIAM1, Rac activation and cell migration | journal = Oncogene | volume = 34 | issue = 2 | pages = 188–98 | date = Jan 2015 | pmid = 24362520 | doi = 10.1038/onc.2013.549 | pmc=4067478}}
38. ^{{cite journal | vauthors = Theendakara V, Patent A, Peters Libeu CA, Philpot B, Flores S, Descamps O, Poksay KS, Zhang Q, Cailing G, Hart M, John V, Rao RV, Bredesen DE | title = Neuroprotective Sirtuin ratio reversed by ApoE4 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 110 | issue = 45 | pages = 18303–08 | date = Nov 2013 | pmid = 24145446 | doi = 10.1073/pnas.1314145110 | pmc=3831497| bibcode = 2013PNAS..11018303T }}
39. ^{{cite journal | vauthors = van Leeuwen IM, Higgins M, Campbell J, McCarthy AR, Sachweh MC, Navarro AM, Laín S | title = Modulation of p53 C-terminal acetylation by mdm2, p14ARF, and cytoplasmic SirT2 | journal = Molecular Cancer Therapeutics | volume = 12 | issue = 4 | pages = 471–80 | date = Apr 2013 | pmid = 23416275 | doi = 10.1158/1535-7163.MCT-12-0904 }}
40. ^{{cite journal | vauthors = Jiang W, Wang S, Xiao M, Lin Y, Zhou L, Lei Q, Xiong Y, Guan KL, Zhao S | title = Acetylation regulates gluconeogenesis by promoting PEPCK1 degradation via recruiting the UBR5 ubiquitin ligase | journal = Molecular Cell | volume = 43 | issue = 1 | pages = 33–44 | date = Jul 2011 | pmid = 21726808 | doi = 10.1016/j.molcel.2011.04.028 | pmc=3962309}}
41. ^{{cite journal | vauthors = Wang F, Tong Q | title = SIRT2 suppresses adipocyte differentiation by deacetylating FOXO1 and enhancing FOXO1's repressive interaction with PPARgamma | journal = Molecular Biology of the Cell | volume = 20 | issue = 3 | pages = 801–08 | date = Feb 2009 | pmid = 19037106 | doi = 10.1091/mbc.E08-06-0647 | pmc=2633403}}
42. ^{{cite journal | vauthors = Han Y, Jin YH, Kim YJ, Kang BY, Choi HJ, Kim DW, Yeo CY, Lee KY | title = Acetylation of Sirt2 by p300 attenuates its deacetylase activity | journal = Biochemical and Biophysical Research Communications | volume = 375 | issue = 4 | pages = 576–80 | date = Oct 2008 | pmid = 18722353 | doi = 10.1016/j.bbrc.2008.08.042 }}
43. ^{{cite journal | vauthors = Jin YH, Kim YJ, Kim DW, Baek KH, Kang BY, Yeo CY, Lee KY | title = Sirt2 interacts with 14-3-3 beta/gamma and down-regulates the activity of p53 | journal = Biochemical and Biophysical Research Communications | volume = 368 | issue = 3 | pages = 690–5 | date = Apr 2008 | pmid = 18249187 | doi = 10.1016/j.bbrc.2008.01.114 }}
44. ^{{cite journal | vauthors = Shimazu T, Horinouchi S, Yoshida M | title = Multiple histone deacetylases and the CREB-binding protein regulate pre-mRNA 3'-end processing | journal = The Journal of Biological Chemistry | volume = 282 | issue = 7 | pages = 4470–78 | date = Feb 2007 | pmid = 17172643 | doi = 10.1074/jbc.M609745200 }}

Further reading

{{refbegin|33em}}
  • {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides | journal = Gene | volume = 138 | issue = 1–2 | pages = 171–74 | date = Jan 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
  • {{cite journal | vauthors = Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA | title = A "double adaptor" method for improved shotgun library construction | journal = Analytical Biochemistry | volume = 236 | issue = 1 | pages = 107–13 | date = Apr 1996 | pmid = 8619474 | doi = 10.1006/abio.1996.0138 }}
  • {{cite journal | vauthors = Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA | title = Large-scale concatenation cDNA sequencing | journal = Genome Research | volume = 7 | issue = 4 | pages = 353–58 | date = Apr 1997 | pmid = 9110174 | pmc = 139146 | doi = 10.1101/gr.7.4.353 }}
  • {{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1–2 | pages = 149–56 | date = Oct 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}
  • {{cite journal | vauthors = Frye RA | title = Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins | journal = Biochemical and Biophysical Research Communications | volume = 273 | issue = 2 | pages = 793–98 | date = Jul 2000 | pmid = 10873683 | doi = 10.1006/bbrc.2000.3000 }}
  • {{cite journal | vauthors = Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL | title = Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 97 | issue = 17 | pages = 9543–48 | date = Aug 2000 | pmid = 10931946 | pmc = 16901 | doi = 10.1073/pnas.160270997 | bibcode = 2000PNAS...97.9543H }}
  • {{cite journal | vauthors = Finnin MS, Donigian JR, Pavletich NP | title = Structure of the histone deacetylase SIRT2 | journal = Nature Structural Biology | volume = 8 | issue = 7 | pages = 621–25 | date = Jul 2001 | pmid = 11427894 | doi = 10.1038/89668 }}
  • {{cite journal | vauthors = Grozinger CM, Chao ED, Blackwell HE, Moazed D, Schreiber SL | title = Identification of a class of small molecule inhibitors of the sirtuin family of NAD-dependent deacetylases by phenotypic screening | journal = The Journal of Biological Chemistry | volume = 276 | issue = 42 | pages = 38837–43 | date = Oct 2001 | pmid = 11483616 | doi = 10.1074/jbc.M106779200 }}
  • {{cite journal | vauthors = Borra MT, O'Neill FJ, Jackson MD, Marshall B, Verdin E, Foltz KR, Denu JM | title = Conserved enzymatic production and biological effect of O-acetyl-ADP-ribose by silent information regulator 2-like NAD+-dependent deacetylases | journal = The Journal of Biological Chemistry | volume = 277 | issue = 15 | pages = 12632–41 | date = Apr 2002 | pmid = 11812793 | doi = 10.1074/jbc.M111830200 }}
  • {{cite journal | vauthors = De Smet C, Nishimori H, Furnari FB, Bögler O, Huang HJ, Cavenee WK | title = A novel seven transmembrane receptor induced during the early steps of astrocyte differentiation identified by differential expression | journal = Journal of Neurochemistry | volume = 81 | issue = 3 | pages = 575–88 | date = May 2002 | pmid = 12065666 | doi = 10.1046/j.1471-4159.2002.00847.x }}
  • {{cite journal | vauthors = North BJ, Marshall BL, Borra MT, Denu JM, Verdin E | title = The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase | journal = Molecular Cell | volume = 11 | issue = 2 | pages = 437–44 | date = Feb 2003 | pmid = 12620231 | doi = 10.1016/S1097-2765(03)00038-8 }}
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  • {{cite journal | vauthors = de Oliveira RM, Sarkander J, Kazantsev AG, Outeiro TF | title = SIRT2 as a Therapeutic Target for Age-Related Disorders | journal = Frontiers in Pharmacology | volume = 3 | issue = | page = 82 | year = 2012 | pmid = 22563317 | pmc = 3342661 | doi = 10.3389/fphar.2012.00082 }}
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1 : Genes mutated in mice
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