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

David Olson, Namrata D. Udeshi, Noah A. Wolfson, Carol Ann Pitcairn, Eric D. Sullivan, Jacob D. Jaffe, Tanya Svinkina, Ted Natoli, Xiaodong Lu, Joshiawa Paulk, Patrick McCarren, Florence F. Wagner, Doug Barker, Eleanor Howe, Fanny Lazzaro, Jennifer P. Gale, Yan Ling Zhang, Aravind Subramanian, Carol A. Fierke, Steven A. CarrEdward B. Holson

Research output: Contribution to journalArticlepeer-review

57 Scopus citations


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. (Chemical Presented).

Original languageEnglish (US)
Pages (from-to)2210-2216
Number of pages7
JournalACS Chemical Biology
Issue number10
StatePublished - Oct 17 2014
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine


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