An Unbiased Approach To Identify Endogenous Substrates of “Histone” Deacetylase 8
ACS Chemical Biology2014Vol. 9(10), pp. 2210–2216
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David E. Olson, Namrata D. Udeshi, Noah A. Wolfson, Carol Ann Pitcairn, Eric D. Sullivan, Jacob D. Jaffe, Tanya Svinkina, Ted Natoli, Xiaodong Lü, Joshiawa Paulk, Patrick McCarren, Florence F. Wagner, Doug Barker, Eleanor Howe, Fanny Lazzaro, Jennifer Gale, Yan-Ling Zhang, Aravind Subramanian, Carol A. Fierke, Steven A. Carr, Edward B. Holson
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.
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