SIRT1 interacts with p73 and suppresses p73-dependent transcriptional activity.

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Dai JM, Wang ZY, Sun DC, Lin RX, Wang SQ

SIRT1 interacts with p73 and suppresses p73-dependent transcriptional activity.

J Cell Physiol. 2007 Jan;210(1):161-6.

PubMed ID

16998810 [ View in PubMed

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Abstract

The tumor suppressor p53-related p73 shares significant amino-acid sequence identity with p53. Like p53, p73 recognizes canonical p53 DNA-binding sites and activates p53-responsive target genes and induces apoptosis. Moreover, SIRT1 binds to p53 while repressing the expression of their target genes. Here, we report that SIRT1 also binds to p73 and suppresses p73-dependent transcriptional activity. SIRT1 in human cells reduces the transcriptional activity of p73, and partly inhibits apoptosis induced by p73. Furthermore, SIRT1 can deacetylate p73 protein acetylation both in vivo and in vitro. Collectively, these data suggest that SIRT1 can modulate p73 activity via deacetylation.

DrugBank Data that Cites this Article

Polypeptides

Name	UniProt ID
NAD-dependent protein deacetylase sirtuin-1	Q96EB6	Details

Pharmaco-transcriptomics

Drug	Drug Groups	Gene	Gene ID	Change	Interaction	Chromosome
Resveratrol	Investigational	BAX	581	downregulated	resveratrol results in decreased expression of BAX mRNA	19q13.33
Resveratrol	Investigational	MDM2	4193	downregulated	resveratrol results in decreased expression of MDM2 mRNA	12q15
Nicotinamide	Approved Investigational	BAX	581	upregulated	Niacinamide results in increased expression of BAX mRNA	19q13.33
Nicotinamide	Approved Investigational	MDM2	4193	upregulated	Niacinamide results in increased expression of MDM2 mRNA	12q15