Acetylation of Sirt2 by p300 attenuates its deacetylase activity

Han, Younho; Jin, Yipeng; Kim, Yeon Jin; Kang, Bok Yun; Choi, Hyun Jin; Kim, Dae Won; Yeo, Chang Yeol; Lee, Kwang Youl

doi:10.1016/j.bbrc.2008.08.042

Cited by 85 publications

(54 citation statements)

References 23 publications

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“…p300 has been shown to acetylate SIRT2, interfering with its catalytic activity. 16 Thus, inhibition of SIRT1 could lead to SIRT2 inhibition through the activity of p300. It is possible that the normal cellular distribution of these proteins minimizes the effects of these potential interactions, with SIRT1 primarily in the nucleus and SIRT2 primarily in the cytoplasm, necessitating a nuclear-cytoplasmic shuttling of p300 to achieve SIRT2 inhibition as a downstream effect of SIRT1 inhibition.…”

Section: Resultsmentioning

confidence: 99%

Sirtuin deacetylases: A new target for melanoma management

et al. 2014

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y These authors contributed equally to this work.M elanoma continues to cause more deaths than any other skin cancer, necessitating the development of new avenues of treatment. One promising new opportunity comes in the form of mechanism-based therapeutic targets. We recently reported the overexpression and delocalization of the class III histone deacetylase SIRT1 in melanoma, and demonstrated that its small molecule inhibition via Tenovin-1 decreased cell growth and viability of melanoma cells, possibly by a p53 mediated induction of p21. Here, we support our data using additional SIRT inhibitors, viz. Sirtinol and Ex-527, which suggests possible benefits of concomitantly inhibiting more than one Sirtuin for an effective cancer management strategy. This "Extra View" paper also includes a discussion of our results in the context of similar recent and concurrent studies. Furthermore, we expand upon our findings in an analysis of new research that may link the cellular localization and growth effects of SIRT1 with the PI3K signaling pathway.

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Section: Resultsmentioning

confidence: 99%

Sirtuin deacetylases: A new target for melanoma management

et al. 2014

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“…However, the influence of SIRT2 on p300 appears to be opposite to that of SIRT1 [18], as mentioned above in the context of p53 degradation. In turn, p300 inhibits SIRT2 through acetylation, attenuating its negative influence on p53 [73].…”

Section: Transcriptional and Post-transcriptional Regulators As Sirtumentioning

confidence: 99%

Sirtuins and their interactions with transcription factors and poly(ADP-ribose) polymerases

Jęśko¹,

Strosznajder²

2016

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A b s t r a c tSirtuins vast number of targets in many cellular compartments, and some display additional enzymatic activities including mono(ADP-ribosyl)ation. SIRTs interact with multiple signalling proteins, transcription factors and enzymes including p53, FOXOs (forkhead box subgroup O), PPARs (peroxisome proliferator-activated receptors), NF-κB, and DNA-PK (DNA-dependent protein kinase). Sirtuins also interact extensively with the family of poly(ADPribose) polymerases (PARPs), a crucial and widespread class of NAD

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“…In line with this, the bacterial sirtuin CobB was also shown to lack the corresponding helix but remained an active sirtuin [146]. Interestingly, SIRT2 isoform 5 retained the ability to associate with P300, a known target of SIRT2 [58,147].…”

Section: The Nuclear Isoform Of Sirt2 Does Not Deacetylate Nuclear Tamentioning

confidence: 90%