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Gene Review

SIRT2  -  sirtuin 2

Homo sapiens

Synonyms: NAD-dependent protein deacetylase sirtuin-2, Regulatory protein SIR2 homolog 2, SIR2, SIR2-like protein 2, SIR2L, ...
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Disease relevance of SIRT2

  • SIRT2 is located at 19q13.2, a region known to be frequently deleted in human gliomas [1].
  • Since it is however severely reduced in a large number of human brain tumor cell lines, the absence of SIRT2, a potential tumor suppressor, could play a key role in the regulation of the cell-cycle within a multistep pathway that leads to full cellular transformation and, finally, the development of cellular malignancy [2].

High impact information on SIRT2

  • Here, we report that a human ortholog of Sir2p, sirtuin type 2 (SIRT2), is a predominantly cytoplasmic protein that colocalizes with microtubules [3].
  • SIRT2 deacetylates lysine-40 of alpha-tubulin both in vitro and in vivo [3].
  • CDC14B may provoke exit from mitosis coincident with the loss of SIRT2 via ubiquitination and subsequent degradation by the 26S proteasome [4].
  • Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle [4].
  • A CDC14B mutant defective in catalyzing dephosphorylation fails to change the phosphorylation status or abundance of SIRT2 protein [4].

Biological context of SIRT2

  • Cells stably overexpressing the wild-type SIRT2 but not missense mutants lacking NDAC activity show a marked prolongation of the mitotic phase of the cell cycle [4].
  • The SIRT2 protein is a NAD-dependent deacetylase (NDAC), the abundance of which increases dramatically during mitosis and is multiply phosphorylated at the G(2)/M transition of the cell cycle [4].
  • Using cell-based assays and RNA interference, we show that puromycin-induced cell death is greatly diminished by nicotinamide (a potent sirtuin inhibitor), and by decreased expression of sirtuins SIRT2 and SIRT3 [5].
  • Our identification of putative nuclear export sequences in numerous vertebrate SIRT2 proteins shows that active nuclear export can be a conserved mechanism for regulating Sir2 homologues [6].
  • Determination of the exon-intron splice junctions found the full-length SIRT2 protein to consist of 16 exons ranging in size from 16 bp (exon 1) to 749 bp (exon 9) [2].

Associations of SIRT2 with chemical compounds

  • On the basis of our results, a phenol moiety on the active compound is suggested to be important for SIRT2 inhibitory activity [7].

Co-localisations of SIRT2


Other interactions of SIRT2

  • Hereby, we describe the identification of a compound we named cambinol that inhibits NAD-dependent deacetylase activity of human SIRT1 and SIRT2 [8].
  • FISH-mapping and genomic organization of the NAD-dependent histone deacetylase gene, Sirtuin 2 (Sirt2) [2].
  • Taken together, the findings may represent or lead to cytoskeletal impairment; aberrant antioxidant proteins, chaperons, MAP kinase kinase 1 and NAD-dependent deacetylase sirtuin-2 may have been involved in pathogenetic mechanisms and altered synaptosomal protein expression possibly reflects synaptic impairment in MTLE [9].

Analytical, diagnostic and therapeutic context of SIRT2


  1. Proteomics-based identification of differentially expressed genes in human gliomas: down-regulation of SIRT2 gene. Hiratsuka, M., Inoue, T., Toda, T., Kimura, N., Shirayoshi, Y., Kamitani, H., Watanabe, T., Ohama, E., Tahimic, C.G., Kurimasa, A., Oshimura, M. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  2. FISH-mapping and genomic organization of the NAD-dependent histone deacetylase gene, Sirtuin 2 (Sirt2). Voelter-Mahlknecht, S., Ho, A.D., Mahlknecht, U. Int. J. Oncol. (2005) [Pubmed]
  3. The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. North, B.J., Marshall, B.L., Borra, M.T., Denu, J.M., Verdin, E. Mol. Cell (2003) [Pubmed]
  4. Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle. Dryden, S.C., Nahhas, F.A., Nowak, J.E., Goustin, A.S., Tainsky, M.A. Mol. Cell. Biol. (2003) [Pubmed]
  5. Metabolite of SIR2 reaction modulates TRPM2 ion channel. Grubisha, O., Rafty, L.A., Takanishi, C.L., Xu, X., Tong, L., Perraud, A.L., Scharenberg, A.M., Denu, J.M. J. Biol. Chem. (2006) [Pubmed]
  6. Nuclear export modulates the cytoplasmic Sir2 homologue Hst2. Wilson, J.M., Le, V.Q., Zimmerman, C., Marmorstein, R., Pillus, L. EMBO Rep. (2006) [Pubmed]
  7. An in silico approach to discovering novel inhibitors of human sirtuin type 2. Tervo, A.J., Kyrylenko, S., Niskanen, P., Salminen, A., Leppänen, J., Nyrönen, T.H., Järvinen, T., Poso, A. J. Med. Chem. (2004) [Pubmed]
  8. Antitumor activity of a small-molecule inhibitor of human silent information regulator 2 enzymes. Heltweg, B., Gatbonton, T., Schuler, A.D., Posakony, J., Li, H., Goehle, S., Kollipara, R., Depinho, R.A., Gu, Y., Simon, J.A., Bedalov, A. Cancer Res. (2006) [Pubmed]
  9. Aberrant expression of cytoskeleton proteins in hippocampus from patients with mesial temporal lobe epilepsy. Yang, J.W., Czech, T., Felizardo, M., Baumgartner, C., Lubec, G. Amino Acids (2006) [Pubmed]
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