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Bromodomains (BRDs) are conserved protein interaction modules which recognize (read) acetyl-lysine modifications, however their role(s) in regulating cellular states and their potential as targets for the development of targeted treatment strategies is poorly understood. Here we present a set of 25 chemical probes, selective small molecule inhibitors, covering 29 human bromodomain targets. We comprehensively evaluate the selectivity of this probe-set using BROMOscan and demonstrate the utility of the set identifying roles of BRDs in cellular processes and potential translational applications. For instance, we discovered crosstalk between histone acetylation and the glycolytic pathway resulting in a vulnerability of breast cancer cell lines under conditions of glucose deprivation or GLUT1 inhibition to inhibition of BRPF2/3 BRDs. This chemical probe-set will serve as a resource for future applications in the discovery of new physiological roles of bromodomain proteins in normal and disease states, and as a toolset for bromodomain target validation.

Original publication

DOI

10.1038/s41467-019-09672-2

Type

Journal article

Journal

Nat Commun

Publication Date

23/04/2019

Volume

10

Keywords

Acetylation, Amino Acid Sequence, Antineoplastic Agents, Cell Line, Tumor, Epigenesis, Genetic, Epithelial Cells, Gene Expression Regulation, Neoplastic, Glucose, Glucose Transporter Type 1, Glycolysis, High-Throughput Screening Assays, Histone Acetyltransferases, Histone Chaperones, Histones, Humans, Mammary Glands, Human, Nuclear Proteins, Protein Processing, Post-Translational, Signal Transduction, Small Molecule Libraries, Structure-Activity Relationship