Sirtuin 2
SIRT2 | |||||||||||||
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Aliases | SIRT2, SIR2, SIR2L, SIR2L2, sirtuin 2 | ||||||||||||
External IDs | OMIM: 604480 MGI: 1927664 HomoloGene: 40823 GeneCards: SIRT2 | ||||||||||||
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Species | Human | Mouse | |||||||||||
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RefSeq (protein) | |||||||||||||
Location (UCSC) | Chr 19: 38.88 – 38.9 Mb | Chr 7: 28.77 – 28.79 Mb | |||||||||||
PubMed search | [3] | [4] | |||||||||||
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NAD-dependent deacetylase sirtuin 2 is an enzyme that in humans is encoded by the SIRT2 gene.[5][6][7] 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.[8] 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.[9]
Function[]
Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity.[7] Cytosolic functions of SIRT2 include the regulation of microtubule acetylation, control of myelination in the central and peripheral nervous system[citation needed] and gluconeogenesis.[10] 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.[11] In response to DNA damage, SIRT2 was also found to deacetylate H3K56 in vivo.[12] Finally, SIRT2 negatively regulates the acetyltransferase activity of the transcriptional co-activator p300 via deacetylation of an automodification loop within its catalytic domain.[13]
Structure[]
Gene[]
Human SIRT2 gene has 18 exons resides on chromosome 19 at q13.[7] For SIRT2, four different human splice variants are deposited in the GenBank sequence database.[14]
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.[7] 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.[14] Since deletion of the NES led to nucleocytoplasmic distribution, it is suggested to mediate their cytosolic localization.[15]
Selective ligands[]
Inhibitors[]
- Benzamide compound # 64[16]
- (S)-2-Pentyl-6-chloro,8-bromo-chroman-4-one: IC50 of 1.5 μM, highly selective over SIRT2 and SIRT3[17]
- 3′-Phenethyloxy-2-anilinobenzamide (33i): IC50 of 0.57 μM[18]
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[20][21] 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.[22][23][24] Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[19][25] Twenty five tests were carried out on homozygous mutant adult mice, however no significant abnormalities were observed.[19]
Animal studies[]
Metabolic actions[]
SIRT2 suppresses inflammatory responses in mice through p65 deacetylation and inhibition of NF-κB activity.[26] 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.[27]
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.[28][29] In addition, recent evidence shows that inhibition of SIRT2 protects against MPTP-induced neuronal loss in vivo.[30]
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),[31] thereby regulating chromosomal condensation during mitosis.[32] During the cell cycle, SIRT2 associates with several mitotic structures including the centrosome, mitotic spindle, and midbody, presumably to ensure normal cell division.[15] Finally, cells with SIRT2 overexpression exhibit marked prolongation of the cell cycle.[33]
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.[34] SIRT2-specific inhibitors exhibits broad anticancer activity.[35][36]
Interactions[]
SIRT2 has been shown to interact with:
- α-tubulin,[37]
- TUG,[38]
- β-catenin,[39]
- PGAM2,[40]
- TIAM1,[41]
- ApoE4,[42]
- p53,[43]
- PEPCK,[44]
- FOXO1,[45]
- p300,[46]
- 14-3-3 protein,[47]
- G6PD,[27][36] and
- CBP.[48]
References[]
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Further reading[]
- Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–74. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (Apr 1996). "A "double adaptor" method for improved shotgun library construction". Analytical Biochemistry. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
- Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA (Apr 1997). "Large-scale concatenation cDNA sequencing". Genome Research. 7 (4): 353–58. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- Frye RA (Jul 2000). "Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins". Biochemical and Biophysical Research Communications. 273 (2): 793–98. doi:10.1006/bbrc.2000.3000. PMID 10873683.
- 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 (Aug 2000). "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning". Proceedings of the National Academy of Sciences of the United States of America. 97 (17): 9543–48. Bibcode:2000PNAS...97.9543H. doi:10.1073/pnas.160270997. PMC 16901. PMID 10931946.
- Finnin MS, Donigian JR, Pavletich NP (Jul 2001). "Structure of the histone deacetylase SIRT2". Nature Structural Biology. 8 (7): 621–25. doi:10.1038/89668. PMID 11427894. S2CID 27800665.
- Grozinger CM, Chao ED, Blackwell HE, Moazed D, Schreiber SL (Oct 2001). "Identification of a class of small molecule inhibitors of the sirtuin family of NAD-dependent deacetylases by phenotypic screening". The Journal of Biological Chemistry. 276 (42): 38837–43. doi:10.1074/jbc.M106779200. PMID 11483616.
- Borra MT, O'Neill FJ, Jackson MD, Marshall B, Verdin E, Foltz KR, Denu JM (Apr 2002). "Conserved enzymatic production and biological effect of O-acetyl-ADP-ribose by silent information regulator 2-like NAD+-dependent deacetylases". The Journal of Biological Chemistry. 277 (15): 12632–41. doi:10.1074/jbc.M111830200. PMID 11812793.
- De Smet C, Nishimori H, Furnari FB, Bögler O, Huang HJ, Cavenee WK (May 2002). "A novel seven transmembrane receptor induced during the early steps of astrocyte differentiation identified by differential expression". Journal of Neurochemistry. 81 (3): 575–88. doi:10.1046/j.1471-4159.2002.00847.x. PMID 12065666. S2CID 23925334.
- North BJ, Marshall BL, Borra MT, Denu JM, Verdin E (Feb 2003). "The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase". Molecular Cell. 11 (2): 437–44. doi:10.1016/S1097-2765(03)00038-8. PMID 12620231.
- Dryden SC, Nahhas FA, Nowak JE, Goustin AS, Tainsky MA (May 2003). "Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle". Molecular and Cellular Biology. 23 (9): 3173–85. doi:10.1128/MCB.23.9.3173-3185.2003. PMC 153197. PMID 12697818.
- Fulco M, Schiltz RL, Iezzi S, King MT, Zhao P, Kashiwaya Y, Hoffman E, Veech RL, Sartorelli V (Jul 2003). "Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state". Molecular Cell. 12 (1): 51–62. doi:10.1016/S1097-2765(03)00226-0. PMID 12887892.
- Hiratsuka M, Inoue T, Toda T, Kimura N, Shirayoshi Y, Kamitani H, Watanabe T, Ohama E, Tahimic CG, Kurimasa A, Oshimura M (Sep 2003). "Proteomics-based identification of differentially expressed genes in human gliomas: down-regulation of SIRT2 gene" (PDF). Biochemical and Biophysical Research Communications. 309 (3): 558–66. doi:10.1016/j.bbrc.2003.08.029. PMID 12963026.
- van der Horst A, Tertoolen LG, de Vries-Smits LM, Frye RA, Medema RH, Burgering BM (Jul 2004). "FOXO4 is acetylated upon peroxide stress and deacetylated by the longevity protein hSir2(SIRT1)". The Journal of Biological Chemistry. 279 (28): 28873–79. doi:10.1074/jbc.M401138200. PMID 15126506.
- Bae NS, Swanson MJ, Vassilev A, Howard BH (Jun 2004). "Human histone deacetylase SIRT2 interacts with the homeobox transcription factor HOXA10". Journal of Biochemistry. 135 (6): 695–700. doi:10.1093/jb/mvh084. PMID 15213244.
- de Oliveira RM, Sarkander J, Kazantsev AG, Outeiro TF (2012). "SIRT2 as a Therapeutic Target for Age-Related Disorders". Frontiers in Pharmacology. 3: 82. doi:10.3389/fphar.2012.00082. PMC 3342661. PMID 22563317.
External links[]
- Genes on human chromosome 19
- Genes mutated in mice