4.7 Article

SIRT1 interacts with p73 and suppresses p73-dependent transcriptional activity

Journal

JOURNAL OF CELLULAR PHYSIOLOGY
Volume 210, Issue 1, Pages 161-166

Publisher

WILEY
DOI: 10.1002/jcp.20831

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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.

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