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Sirtuin1 (SIRT1) in the Acetylation of Downstream Target Proteins

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Histone Deacetylases

Part of the book series: Methods in Molecular Biology ((MIMB,volume 1436))

Abstract

Acetylation has been shown to be an important posttranslational modification (PTM) of both histone and nonhistone proteins with particular implications in cell signaling and transcriptional regulation of gene expression. Many studies have already demonstrated that SIRT1 is able to deacetylate histones and lead to gene silencing. It can also regulate the function of tumor suppressors including FOXO proteins and p53 by deacetylation. Here, we describe three experimental approaches for studying the modulation of the acetylation status of some of the known downstream targets of SIRT1.

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Authors and Affiliations

  1. Department of Surgery and Cancer, Imperial College London, Hammersmith Hospital Campus, London Du Cane Road, London, W12 0NN, UK

    Ana R. Gomes, Jay Sze Yong, Khai Cheng Kiew, Ebru Aydin, Mattaka Khongkow, Sasiwan Laohasinnarong & Eric W.-F. Lam

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  1. Ana R. Gomes
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  2. Jay Sze Yong
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  3. Khai Cheng Kiew
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  4. Ebru Aydin
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  5. Mattaka Khongkow
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  6. Sasiwan Laohasinnarong
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  7. Eric W.-F. Lam
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Corresponding author

Correspondence to Eric W.-F. Lam .

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Editors and Affiliations

  1. Boston University School of Medicine, Boston, Massachusetts, USA

    Sibaji Sarkar

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Gomes, A.R. et al. (2016). Sirtuin1 (SIRT1) in the Acetylation of Downstream Target Proteins. In: Sarkar, S. (eds) Histone Deacetylases. Methods in Molecular Biology, vol 1436. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-3667-0_12

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  • DOI: https://doi.org/10.1007/978-1-4939-3667-0_12

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  • Publisher Name: Humana Press, New York, NY

  • Print ISBN: 978-1-4939-3665-6

  • Online ISBN: 978-1-4939-3667-0

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