SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis.

By A. Vaquero, Michael B Scher, Dong Hoon Lee, A. Sutton, Hwei-Ling Cheng, F. Alt, Lourdes Serrano, R. Sternglanz, D. Reinberg. Genes & Development, 2006

670 citations recorded by the source corpus.

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 G2/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.

Subfields: Aging, Geriatrics and Gerontology, Oncology

View Paper: https://www.semanticscholar.org/paper/ea5fbbdac00e6788db0548f9de48fea5545f99b8

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Aging

1. M. Haigis
2. E. Verdin
3. Johan Auwerx
4. E. Seto
5. C. Cantó
6. L. Guarente
7. R. Houtkooper
8. Bor Luen Tang

In Geriatrics and Gerontology

1. Johan Auwerx
2. C. Cantó
3. E. Verdin
4. Bor Luen Tang
5. R. Houtkooper
6. M. Haigis
7. E. Seto
8. L. Guarente

In Oncology

1. Johan Auwerx
2. C. Cantó
3. Bor Luen Tang
4. E. Verdin
5. E. Seto
6. R. Houtkooper
7. L. Guarente
8. M. Haigis

Citations in the corpus

• Mammalian sirtuins--emerging roles in physiology, aging, and calorie restriction. (2006, background): “SIRT2 colocalizes with chromatin during the G 2 /M transition, a period in which the nuclear membrane has broken down (Vaquero et al. 2006).”
• Sirt1 and the Mitochondria (2016, background): “, 2005), and it is not just a bona fide histone deacetylase (Vaquero et al., 2006) but also deacetylates histone modifying enzymes such as the histone methyl-transferase SUV39H1 (Vaquero et al.”
• Sirtuins: critical regulators at the crossroads between cancer and aging (2007, background): “In the nucleus, SIRT2 deacetylates H4-K16, and during the G2/M transition, global levels of H4-K16 acetylation decrease, which may aid in chromatin condensation (Vaquero et al., 2006).”
• Sirtuins as regulators of metabolism and healthspan (2012, background): “SIRT2 is considered to be cytosolic but is also present in the nucleus in the G2 phase to M phase transition of the cell cycl”
• The secret life of NAD+: an old metabolite controlling new metabolic signaling pathways. (2010, background): “In contrast, SIRT2 is mainly localized in the cytoplasm, although it can also regulate gene expression by deacetylating transcription factors that shuttle from the cytoplasm to the nucleus (68), and it contributes to chromatin compaction upon disassembly of the cell nucleus during mitosis (69).”
• Erasers of histone acetylation: the histone deacetylase enzymes. (2014, background): “Although there are reports that SIRT1 can deacetylate all four core histones in vitro, SIRT1’s chief target site on histones is H4K16 (Vaquero et al. 2004).”