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

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.

journal_name

ACS Chem Biol

journal_title

ACS chemical biology

authors

Olson 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

doi

10.1021/cb500492r

subject

Has Abstract

pub_date

2014-10-17 00:00:00

pages

2210-6

issue

10

eissn

1554-8929

issn

1554-8937

journal_volume

9

pub_type

信件

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