hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase.

Article Details

Citation

Vaziri H, Dessain SK, Ng Eaton E, Imai SI, Frye RA, Pandita TK, Guarente L, Weinberg RA

hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase.

Cell. 2001 Oct 19;107(2):149-59.

PubMed ID
11672523 [ View in PubMed
]
Abstract

DNA damage-induced acetylation of p53 protein leads to its activation and either growth arrest or apoptosis. We show here that the protein product of the gene hSIR2(SIRT1), the human homolog of the S. cerevisiae Sir2 protein known to be involved in cell aging and in the response to DNA damage, binds and deacetylates the p53 protein with a specificity for its C-terminal Lys382 residue, modification of which has been implicated in the activation of p53 as a transcription factor. Expression of wild-type hSir2 in human cells reduces the transcriptional activity of p53. In contrast, expression of a catalytically inactive hSir2 protein potentiates p53-dependent apoptosis and radiosensitivity. We propose that hSir2 is involved in the regulation of p53 function via deacetylation.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
NAD-dependent protein deacetylase sirtuin-1Q96EB6Details
Cellular tumor antigen p53P04637Details