The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis
Open accessAbstract
The mammalian cytoplasmic protein SirT2 is a member of the Sir2 family of NAD+-dependent protein deacetylases involved in caloric restriction-dependent life span extension. We found that SirT2 and its yeast counterpart Hst2 have a strong preference for histone H4K16Ac in their deacetylation activity in vitro and in vivo. We have pinpointed the decrease in global levels of H4K16Ac during the mammalian cell cycle to the G 2/M transition that coincides with SirT2 localization on chromatin. Mouse embryonic fibroblasts (MEFs) deficient for SirT2 show higher levels of H4K16Ac in mitosis, in contrast to the normal levels exhibited by SirT1-deficient MEFs. The enzymatic conversion of H4K16Ac to its deacetylated form may be pivotal to the formation of condensed chromatin. Thus, SirT2 is a major contributor to this enzymatic conversion at the time in the cell’s life cycle when condensed chromatin must be generated anew.
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Citations
Cites
Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
Imai, S.-I., Armstrong, C. M., Kaeberlein, M., & Guarente, L. (2000) · Nature · doi:10.1038/35001622 · Cited by 3,510
Kennedy, B. K., Gotta, M., Sinclair, D. A., Mills, K., McNabb, D. S., Murthy, M., Pak, S. M., Laroche, T., Gasser, S. M., & Guarente, L. (1997) · Cell · doi:10.1016/s0092-8674(00)80219-6 · Cited by 375
Cited by
Chromatin modifications and their function
Kouzarides, T. (2007) · Cell · doi:10.1016/j.cell.2007.02.005 · Cited by 10,883
“The fission yeast class III deacetylase Sir2 has some selectivity for H4K16ac, and recently the human Sir family member SirT2 has been demonstrated to have a similar preference (Vaquero et al., 2006).”
InfluentialSirtuins as regulators of metabolism and healthspan
Houtkooper, R. H., Pirinen, E., & Auwerx, J. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3293 · Cited by 2,008
Epigenetic protein families: a new frontier for drug discovery
Arrowsmith, C. H., Bountra, C., Fish, P. V., Lee, K., & Schapira, M. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3674 · Cited by 1,327
Mammalian sirtuins—emerging roles in physiology, aging, and calorie restriction
Haigis, M. C., & Guarente, L. P. (2006) · Genes & Development · doi:10.1101/gad.1467506 · Cited by 1,295
Histone deacetylases and cancer
Glozak, M. A., & Seto, E. (2007) · Oncogene · doi:10.1038/sj.onc.1210610 · Cited by 1,031
Metadata
- Authors
- Vaquero, A., Scher, M. B., Lee, D. H., Sutton, A., Cheng, H.-L., Alt, F. W., Serrano, L., Sternglanz, R., & Reinberg, D.
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2006-04-28
- Volume
- 20
- Issue
- 10
- Pages
- 1256-1261
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- OpenAlex
- W2165105249
- Cited by
- 665
- References
- 2
- Type
- posted content
- Language
- en
- Open access
- diamond
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- Vaquero, A., Scher, M. B., Lee, D. H., Sutton, A., Cheng, H.-L., Alt, F. W., Serrano, L., Sternglanz, R., & Reinberg, D. (2006). SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis. Genes & Development. https://doi.org/10.1101/gad.1412706
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