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ACS chemical biology DOI:10.1021/cb500492r

An unbiased approach to identify endogenous substrates of "histone" deacetylase 8.

Publication TypeJournal Article
Year of Publication2014
AuthorsOlson, DE, Udeshi, ND, Wolfson, NA, Pitcairn, CA, Sullivan, ED, Jaffe, JD, Svinkina, T, Natoli, T, Lu, X, Paulk, J, McCarren, P, Wagner, FF, Barker, D, Howe, E, Lazzaro, F, Gale, JP, Zhang, YL, Subramanian, A, Fierke, CA, Carr, SA, Holson, EB
JournalACS chemical biology
Volume9
Issue10
Pages2210-6
Date Published2014/10/17
ISSN1554-8929
Abstract

Despite being extensively characterized structurally and biochemically, the functional role of histone deacetylase 8 (HDAC8) has remained largely obscure due in part to a lack of known cellular substrates. Herein, we describe an unbiased approach using chemical tools in conjunction with sophisticated proteomics methods to identify novel non-histone nuclear substrates of HDAC8, including the tumor suppressor ARID1A. These newly discovered substrates of HDAC8 are involved in diverse biological processes including mitosis, transcription, chromatin remodeling, and RNA splicing and may help guide therapeutic strategies that target the function of HDAC8.

URLhttp://dx.doi.org/10.1021/cb500492r
DOI10.1021/cb500492r
Pubmed

http://www.ncbi.nlm.nih.gov/pubmed/25089360?dopt=Abstract