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

ACS Chem Biol
Authors
Keywords
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.

Year of Publication
2014
Journal
ACS Chem Biol
Volume
9
Issue
10
Pages
2210-6
Date Published
2014 Oct 17
ISSN
1554-8937
URL
DOI
10.1021/cb500492r
PubMed ID
25089360
PubMed Central ID
PMC4201337
Links
Grant list
GM40602 / GM / NIGMS NIH HHS / United States
U24 CA160034 / CA / NCI NIH HHS / United States
T32 GM008353 / GM / NIGMS NIH HHS / United States
R01HL096738 / HL / NHLBI NIH HHS / United States
R01 HL096738 / HL / NHLBI NIH HHS / United States
HHSN268201000033C / PHS HHS / United States
U54 HG006093 / HG / NHGRI NIH HHS / United States
R01 GM040602 / GM / NIGMS NIH HHS / United States
T32-GM-008597 / GM / NIGMS NIH HHS / United States
HHSN268201000033C / HL / NHLBI NIH HHS / United States
T32-GM-008353 / GM / NIGMS NIH HHS / United States
T32 GM008597 / GM / NIGMS NIH HHS / United States
U24CA160034 / CA / NCI NIH HHS / United States