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HDAC1 Substrate Profiling using Proteomics-Based Substrate Trapping.

ACS Chem Biol; 2018 Nov 13.
Artigo em Inglês | MEDLINE | ID: mdl-30421914
Histone Deacetylase (HDAC) proteins are overexpressed in multiple diseases, including cancer, and have emerged as anticancer drug targets. HDAC proteins regulate cellular processes, such as cell cycle, apoptosis, and cell proliferation, by deacetylating histone and non-histone substrates. Although a plethora of acetylated proteins have been identified using large-scale proteomic approaches, the HDAC proteins responsible for their dynamic deacetylation are poorly studied. For example, few substrates of HDAC1 have been identified, which is mainly due to the scarcity of the substrate identification tools. We recently developed a mutant trapping strategy to identify novel substrates of HDAC1. Herein, we introduce an improved version of the trapping method that uses mass spectrometry-based proteomics to identify multiple substrates simultaneously. Among the substrate hits, CDK1, AIFM1, MSH6 and RuvB-Like1 were identified as likely HDAC1 substrates. These newly discovered HDAC1 substrates are involved in various biological processes, suggesting novel functions of HDAC1 apart from epigenetics. Substrate trapping combined with MS-based proteomics provides an efficient approach to HDAC1 substrate identification and contributes to the full characterization of HDAC function in normal and disease states.