Open AccessAn Unbiased Approach To Identify Endogenous Substrates of “Histone” Deacetylase 8
Author(s) -
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
Publication year - 2014
Publication title -
acs chemical biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.899
H-Index - 111
eISSN - 1554-8937
pISSN - 1554-8929
DOI - 10.1021/cb500492r
Subject(s) - histone deacetylase , histone , biology , chromatin , chromatin remodeling , computational biology , histone deacetylase 2 , rna splicing , hdac8 , bromodomain , histone deacetylase 5 , microbiology and biotechnology , genetics , rna , gene
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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